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4. 689 Pharmacological chaperones improve intradomain stability and interdomain assembly via distinct binding sites to rescue misfolded cystic fibrosis transmembrane conductance regulator

Author

Baatallah, N., primary, Elbahnsi, A., additional, Mornon, J., additional, Chevalier, B., additional, Pranke, I., additional, Servel, N., additional, Zelli, R., additional, Décout, J., additional, Edelman, A., additional, Sermet, I., additional, Callebaut, I., additional, and Hinzpeter, A., additional

Published
2022
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5. WS21.01 AQP5 and CFTR, two genes associated with pseudo-aquagenic palmoplantar keratoderma?

Author

Girodon, E., primary, Lopez, M., additional, Sperelakis-Beedham, B., additional, Bourrat, E., additional, Gaitch, N., additional, Houriez, F., additional, Martinez, B., additional, Fajac, I., additional, Burgel, P.-R., additional, Hickman, G., additional, Audrézet, M.-P., additional, Guerrot, A.-M., additional, Cabet, F., additional, Gerfaud-Valentin, M., additional, Nove-Josserand, R., additional, Raynal, C., additional, Pagin, A., additional, Reboul, M.-P., additional, De Becdelièvre, A., additional, Callebaut, I., additional, and Bienvenu, T., additional

Published
2022
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8. Pharmacological chaperones improve intra-domain stability and inter-domain assembly via distinct binding sites to rescue misfolded CFTR

Author

Baatallah, N., Elbahnsi, Ahmad, Mornon, J. -P, Chevalier, B., Pranke, I., Servel, N., Zelli, R., Décout, J. -L, Edelman, A., Sermet-Gaudelus, I., Callebaut, I., Hinzpeter, A., Baatallah, N., Elbahnsi, Ahmad, Mornon, J. -P, Chevalier, B., Pranke, I., Servel, N., Zelli, R., Décout, J. -L, Edelman, A., Sermet-Gaudelus, I., Callebaut, I., and Hinzpeter, A.

Abstract

Protein misfolding is involved in a large number of diseases, among which cystic fibrosis. Complex intra- and inter-domain folding defects associated with mutations in the cystic fibrosis transmembrane regulator (CFTR) gene, among which p.Phe508del (F508del), have recently become a therapeutical target. Clinically approved correctors such as VX-809, VX-661, and VX-445, rescue mutant protein. However, their binding sites and mechanisms of action are still incompletely understood. Blind docking onto the 3D structures of both the first membrane-spanning domain (MSD1) and the first nucleotide-binding domain (NBD1), followed by molecular dynamics simulations, revealed the presence of two potential VX-809 corrector binding sites which, when mutated, abrogated rescue. Network of amino acids in the lasso helix 2 and the intracellular loops ICL1 and ICL4 allosterically coupled MSD1 and NBD1. Corrector VX-445 also occupied two potential binding sites on MSD1 and NBD1, the latter being shared with VX-809. Binding of both correctors on MSD1 enhanced the allostery between MSD1 and NBD1, hence the increased efficacy of the corrector combination. These correctors improve both intra-domain folding by stabilizing fragile protein–lipid interfaces and inter-domain assembly via distant allosteric couplings. These results provide novel mechanistic insights into the rescue of misfolded proteins by small molecules., QC 20220524

Published
2021
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10. First heterozygous NOP10 mutation in familial pulmonary fibrosis

Author

Kannengiesser, C. Kannengiesser, C. Kannengiesser, C. Manali, E.D. Revy, P. Callebaut, I. Ba, I. Ba, I. Ba, I. Borgel, A. Borgel, A. Oudin, C. Oudin, C. Haritou, A. Haritou, A. Kolilekas, L. Malagari, K. Borie, R. Borie, R. Lainey, E. Boileau, C. Boileau, C. Crestani, B. Crestani, B. Papiris, S.A.

Published
2020

11. Burrowing fauna mediate alternative stable states in the redox cycling of salt marsh sediments

Author

van de Velde, S.J., Hidalgo-Martinez, S., Callebaut, I., Antler, G., James, R.K., Leermakers, M., Meysman, F.J.R., van de Velde, S.J., Hidalgo-Martinez, S., Callebaut, I., Antler, G., James, R.K., Leermakers, M., and Meysman, F.J.R.

Abstract

The East Anglian salt marsh system (UK) has recently generated intriguing data with respect to sediment biogeochemistry. Neighbouring ponds in these salt marshes show two distinct regimes of redox cycling: the sediments are either iron-rich and bioturbated, or they are sulphide-rich and unbioturbated. No conclusive explanation has yet been given for this remarkable spatial co-occurrence. Here, we quantify the geochemical cycling in both pond types, using pore-water analyses and solid-phase speciation. Our results demonstrate that differences in solid-phase carbon and iron inputs are likely small between pond types, and so these cannot act as the direct driver of the observed redox dichotomy. Instead, our results suggest that the presence of bioturbation plays a key role in the transition from sulphur-dominated to iron-dominated sediments. The presence of burrowing fauna in marine sediments stimulates the mineralisation of organic matter, increases the iron cycling and limits the build-up of free sulphide. Overall, we propose that the observed dichotomy in pond geochemistry is due to alternative stable states, which result from non-linear interactions in the sedimentary iron and sulphur cycles that are amplified by bioturbation. This way, small differences in solid phase input can result in very different regimes of redox cycling due to positive feedbacks. This non-linearity in the iron and sulphur cycling could be an inherent feature of marine sediments, and hence, alternative stable states could be present in other systems.

Published
2020

20. patients and knock-out models

Author

Benyelles, M, Episkopou, H, O'Donohue, MF, Kermasson, L, Frange, P, Poulain, F, Belen, FB, Polat, M, Bole-Feysot, C, Langa-Vives, F, Gleizes, PE, de Villartay, JP, Callebaut, I, Decottignies, A, and Revy, P

Subjects
Hoyeraal-Hreidarsson syndrome, p53, PARN, rRNA, shelterin
Abstract

PARN, poly(A)-specific ribonuclease, regulates the turnover of mRNAs and the maturation and stabilization of the hTR RNA component of telomerase. Biallelic PARN mutations were associated with Hoyeraal-Hreidarsson (HH) syndrome, a rare telomere biology disorder that, because of its severity, is likely not exclusively due to hTR down-regulation. Whether PARN deficiency was affecting the expression of telomere-related genes was still unclear. Using cells from two unrelated HH individuals carrying novel PARN mutations and a human PARN knock-out (KO) cell line with inducible PARN complementation, we found that PARN deficiency affects both telomere length and stability and down-regulates the expression of TRF1, TRF2, TPP1, RAP1, and POT1 shelterin transcripts. Down-regulation of dyskerin-encoding DKC1 mRNA was also observed and found to result from p53 activation in PARN-deficient cells. We further showed that PARN deficiency compromises ribosomal RNA biogenesis in patients' fibroblasts and cells from heterozygous Parn KO mice. Homozygous Parn KO however resulted in early embryonic lethality that was not overcome by p53 KO. Our results refine our knowledge on the pleiotropic cellular consequences of PARN deficiency. C1 [Benyelles, Maname; Kermasson, Laetitia; de Villartay, Jean-Pierre; Revy, Patrick] INSERM, UMR 1163, Lab Genome Dynam Immune Syst, Paris, France. [Benyelles, Maname; Kermasson, Laetitia; de Villartay, Jean-Pierre; Revy, Patrick] Paris Descartes Sorbonne Paris Cite Univ, Imagine Inst, Lab Labellise Ligue, Paris, France. [Episkopou, Harikleia; Poulain, Florian; Decottignies, Anabelle] Catholic Univ Louvain, de Duve Inst, Brussels, Belgium. [O'Donohue, Marie-Francoise; Gleizes, Pierre-Emmanuel] Univ Toulouse, Lab Biol Mol Eucaryote, CBI, CNRS,UPS, Toulouse, France. [Frange, Pierre] Univ Paris 05, Sorbonne Paris Cite, EA 7327, Paris, France. [Frange, Pierre] Hop Necker Enfants Malad, AP HP, Lab Microbiol Clin, Paris, France. [Frange, Pierre] Hop Necker Enfants Malad, AP HP, Unite Immunol Hematol & Rhumatol Pediat, Paris, France. [Belen, Fatma Burcu] Baskent Univ, Pediat Hematol, Fac Med, Ankara, Turkey. [Polat, Meltem] Pamukkale Univ, Pediat Infect Dis, Fac Med, Dept Pediat Infect Dis, Denizli, Turkey. [Bole-Feysot, Christine] Paris Descartes Sorbonne Paris Cite Univ, Imagine Inst, Genom Platform, INSERM,UMR 1163, Paris, France. [Bole-Feysot, Christine] INSERM U1163, Imagine Inst Struct Federat Rech Necker, Genom Core Facil, Paris, France. [Langa-Vives, Francina] Inst Pasteur, Ctr Ingn Genet Murine, Paris, France. [Callebaut, Isabelle] Sorbonne Univ, IMPMC, UMR CNRS 7590, Museum Natl Hist Nat, Paris, France.

Published
2019

21. Electrogenic sulfur oxidation drives trace metal cycling in sediments from the Belgian Coastal Zone

Author

Callebaut, I., Van de Velde, S., Gao, Y., Meysman, F., Mees, Jan, Seys, Jan, Faculty of Sciences and Bioengineering Sciences, Chemistry, Earth System Sciences, and Analytical, Environmental & Geo-Chemistry

Subjects
electrogenic sulfur oxidation, cable bacteria, trace metal cycling
Abstract

Recently, a novel process of microbially mediated sulfide oxidation has been discovered [1]. In this process, named electrogenic sulfur oxidation (e-SOx), long filamentous cable bacteria couple the reduction of oxygen near the sediment-water interface to the oxidation of free sulfide and iron sulfides in deeper sediment layers via electrical currents that run over centimetre-wide distances [1,2]. This spatial decoupling of redox reactions generates a distinct pH profile with an alkaline peak just below the sediment water interface and an acidic pH minimum in the deeper sediment layers. These strong alkalinity gradients have been shown to significantly influence the elemental cycling of iron, manganese and carbonate minerals in the upper ~5 cm of the seafloor through the acidic dissolution of pH-sensitive minerals such as iron sulfides and carbonates [3,4]. Metal oxides and sulfide minerals are primary drivers for trace metals cycling [3,5] and thus, e-SOx will likely affect trace metal cycling. Yet, the impact of e-SOx on trace metal cycling is still largely unknown Here we present results from in situ sampling (November 2014), and laboratory sediment incubations from the Belgian Coastal Zone (BCZ, Station 130). By combining the results of the microsensor profiling, pore water analysis and sequential solid phase extractions for trace metals and inorganic sulfur, it is shown that e-SOx is the primary driver of the biogeochemical cycles of cobalt and arsenic in the BCZ. Trace metal cycling is driven by the dissolution of sulfide minerals at depth and the reprecipitation of iron and manganese oxides near the sediment-water interface.

Published
2017

22. EUFOREA Rhinology Research Forum 2016:report of the brainstorming sessions on needs and priorities in rhinitis and rhinosinusitis

Author

Hellings, P W, Akdis, C A, Bachert, C, Bousquet, J., Pugin, B, Adriaensen, G, Advani, R, Agache, I, Anjo, C, Anmolsingh, R, Annoni, E, Bieber, T, Bizaki, A, Braverman, I, Callebaut, I, Castillo Vizuete, J A, Chalermwatanachai, T, Chmielewski, R, Cingi, Cemal, Cools, L, Coppije, C, Cornet, M E, De Boeck, I, De Corso, E, De Greve, G, Doulaptsi, M, Edmiston, R, Erskine, S, Gevaert, E, Gevaert, P, Golebski, K, Hopkins, C, Hox, V, Jaeggi, C, Joos, G, Khwaja, Tina Storm, Kjeldsen, Anette Drøhse, Klimek, L, Koennecke, M, Kortekaas Krohn, I, Krysko, O, Kumar, Bernadette Nimal, Langdon, C, Lange, B, Lekakis, G, Levie, P, Lourijsen, E, Lund, V J, Martens, Kerstin, Mösges, R, Mullol, J., Nyembue, T D, Palkonen, S, Philpott, C, Aguilar-Pimentel, Juan A, Poirrier, A, Pratas, A C, Prokopakis, E, Pujols, L, Rombaux, P, Schmidt-Weber, C B, Segboer, C, Spacova, I, Staikuniene, J, Steelant, B, Steinsvik, E A, Teufelberger, A, Van Gerven, Luuk P A, Van Gool, K., Verbrugge, R, Verhaeghe, B, Virkkula, P, Vlaminck, S, Vries-Uss, E, Wagenmann, M, Zuberbier, T, Seys, S F, and Fokkens, W J

Subjects
Care pathway, Rhinosinusitis, Research, Precision medicine, Rhinitis
Abstract

The first European Rhinology Research Forum organized by the European Forum for Research and Education in Allergy and Airway Diseases (EUFOREA) was held in the Royal Academy of Medicine in Brussels on 17th and 18th November 2016, in collaboration with the European Rhinologic Society (ERS) and the Global Allergy and Asthma European Network (GA2LEN). One hundred and thirty participants (medical doctors from different specialties, researchers, as well as patients and industry representatives) from 27 countries took part in the multiple perspective discussions including brainstorming sessions on care pathways and research needs in rhinitis and rhinosinusitis. The debates started with an overview of the current state of the art, including weaknesses and strengths of the current practices, followed by the identification of essential research needs, thoroughly integrated in the context of Precision Medicine (PM), with personalized care, prediction of success of treatment, participation of the patient and prevention of disease as key principles for improving current clinical practices. This report provides a concise summary of the outcomes of the brainstorming sessions of the European Rhinology Research Forum 2016.

Published
2017

23. EUFOREA Rhinology Research Forum 2016: report of the brainstorming sessions on needs and priorities in rhinitis and rhinosinusitis

Author

Hellings, PW, Akdis, CA, Bachert, C, Bousquet, J, Pugin, B, Adriaensen, G, Advani, R, Agache, I, Anjo, C, Anmolsingh, R, Annoni, E, Bieber, T, Bizaki, A, Braverman, I, Callebaut, I, Castillo Vizuete, JA, Chalermwatanachai, T, Chmielewski, R, Cingi, C, Cools, L, Coppije, C, Cornet, M, De Boeck, I, De Corso, E, De Greve, G, Doulaptsi, M, Erskine, S, Gevaert, E, Gevaert, P, Golebski, K, Hopkins, C, Hox, V, Jaeggi, C, Joos, G, Khwaja, S, Kjeldsen, A, Klimek, L, Koennecke, M, Kortekaas Krohn, I, Krysko, O, Kumar, BN, Langdon, C, Lange, B, Lekakis, G, Levie, P, Lourijsen, E, Lund, V, Martens, K, Mösges, R, Mullol, J, Nyembue, TD, Palkonen, S, Philpott, C, Pimentel, J, Poirrier, A, Pratas, AC, Prokopakis, E, Pujols, L, Rombaux, P, Schmidt-Weber, C, Segboer, C, Spacova, I, Staikuniene, J, Steelant, B, Steinsvik, EA, Teufelberger, A, Van Gerven, L, Van Gool, K, Verbrugge, R, Verhaeghe, B, Virkkula, P, Vlaminck, S, Vries-Uss, E, Wagenmann, M, Zuberbier, T, Seys, SF, and Fokkens, WJ

Abstract

The first European Rhinology Research Forum organized by the European Forum for Research and Education in Allergy and Airway Diseases (EUFOREA) was held in the Royal Academy of Medicine in Brussels on 17th and 18th November 2016, in collaboration with the European Rhinologic Society (ERS) and the Global Allergy and Asthma European Network (GA2LEN). One hundred and thirty participants (medical doctors from different specialties, researchers, as well as patients and industry representatives) from 27 countries took part in the multiple perspective discussions including brainstorming sessions on care pathways and research needs in rhinitis and rhinosinusitis. The debates started with an overview of the current state of the art, including weaknesses and strengths of the current practices, followed by the identification of essential research needs, thoroughly integrated in the context of Precision Medicine (PM), with personalized care, prediction of success of treatment, participation of the patient and prevention of disease as key principles for improving current clinical practices. This report provides a concise summary of the outcomes of the brainstorming sessions of the European Rhinology Research Forum 2016.

Published
2017

25. Impact of electrogenic sulfur oxidation on trace metal cycling in a coastal sediment

Author

van de Velde, S., Callebaut, I., Gao, Y., Meysman, F.J.R., van de Velde, S., Callebaut, I., Gao, Y., and Meysman, F.J.R.

Abstract

Electrogenic sulfur oxidation (e-SOx) is a newly discovered pathway of microbial sulfide oxidation, mediated by so-called cable bacteria. The reduction of oxygen near the sediment-water interface is coupled by long-distance electron transport to the oxidation of sulfide in deeper sediment, and in this way, electrical currents are induced within the seafloor that range over centimeter scale distances. Previously, electrogenic sulfur oxidation has been shown to generate extreme pH excursions in the pore water, and as a result, the process strongly amplifies the cycling of various pH-sensitive minerals, such sulfide minerals and carbonates. Here we show that e-SOx also strongly influence the early diagenesis of trace metals in coastal sediments. For this, field observations at a shallow subtidal site in the North Sea were combined with dedicated laboratory incubations of repacked sediments. High resolution microsensor profiling (pH, H2S and O2) confirmed the typical geochemical signature of e-SOx both in situ as in the laboratory experiments. Pore water analysis revealed a strong mobilization of both arsenic and cobalt within the electro-active sediment zone. The dissolution of iron sulfides, resulting from the acidification of the pore water by e-SOx, appears to be the main driver for the observed release of cobalt and arsenic. The current generated by e-SOx affects charged species. In this manuscript, we have proposed a new estimation method for the associated current density, based on the rate of sulfide oxidation.Overall, electrogenic sulfur oxidation has a major impact on the cycling of arsenic and cobalt in coastal sediments, and may substantially increase the effluxes of these trace metals to the coastal ocean.

Published
2017

26. EUFOREA Rhinology Research Forum 2016: report of the brainstorming sessions on needs and priorities in rhinitis and rhinosinusitis

Author

Hellings, P. W., Akdis, C. A., Bachert, C., Bousquet, J., Pugin, B., Adriaensen, G., Advani, R., Agache, I., Anjo, C., Anmolsingh, R., Annoni, E., Bieber, T., Bizaki, A., Braverman, I., Callebaut, I., Castillo Vizuete, J. A., Chalermwatanachai, T., Chmielewski, R., Cingi, C., Cools, L., Coppije, C., Cornet, M. E., De Boeck, I., De Corso, E., De Greve, G., Doulaptsi, M., Edmiston, R., Erskine, S., Gevaert, E., Gevaert, P., Golebski, K., Hopkins, C., Hox, V., Jaeggi, C., Joos, G., Khwaja, S., Kjeldsen, A., Klimek, L., Koennecke, M., Krohn, I. Kortekaas, Krysko, O., Kumar, B. N., Langdon, C., Lange, B., Lekakis, G., Levie, P., Lourijsen, E., Lund, V. J., Martens, K., Moesges, R., Mullol, J., Nyembue, T. D., Palkonen, S., Philpott, C., Pimentel, J., Poirrier, A., Pratas, A. C., Prokopakis, E., Pujols, L., Rombaux, P., Schmidt-Weber, C., Segboer, C., Spacova, I., Staikuniene, J., Steelant, B., Steinsvik, E. A., Teufelberger, A., Van Gerven, L., Van Gool, K., Verbrugge, R., Verhaeghe, B., Virkkula, P., Vlaminck, S., Vries-Uss, E., Wagenmann, M., Zuberbier, T., Seys, S. F., Fokkens, W. J., Hellings, P. W., Akdis, C. A., Bachert, C., Bousquet, J., Pugin, B., Adriaensen, G., Advani, R., Agache, I., Anjo, C., Anmolsingh, R., Annoni, E., Bieber, T., Bizaki, A., Braverman, I., Callebaut, I., Castillo Vizuete, J. A., Chalermwatanachai, T., Chmielewski, R., Cingi, C., Cools, L., Coppije, C., Cornet, M. E., De Boeck, I., De Corso, E., De Greve, G., Doulaptsi, M., Edmiston, R., Erskine, S., Gevaert, E., Gevaert, P., Golebski, K., Hopkins, C., Hox, V., Jaeggi, C., Joos, G., Khwaja, S., Kjeldsen, A., Klimek, L., Koennecke, M., Krohn, I. Kortekaas, Krysko, O., Kumar, B. N., Langdon, C., Lange, B., Lekakis, G., Levie, P., Lourijsen, E., Lund, V. J., Martens, K., Moesges, R., Mullol, J., Nyembue, T. D., Palkonen, S., Philpott, C., Pimentel, J., Poirrier, A., Pratas, A. C., Prokopakis, E., Pujols, L., Rombaux, P., Schmidt-Weber, C., Segboer, C., Spacova, I., Staikuniene, J., Steelant, B., Steinsvik, E. A., Teufelberger, A., Van Gerven, L., Van Gool, K., Verbrugge, R., Verhaeghe, B., Virkkula, P., Vlaminck, S., Vries-Uss, E., Wagenmann, M., Zuberbier, T., Seys, S. F., and Fokkens, W. J.

Abstract

The first European Rhinology Research Forum organized by the European Forum for Research and Education in Allergy and Airway Diseases (EUFOREA) was held in the Royal Academy of Medicine in Brussels on 17th and 18th November 2016, in collaboration with the European Rhinologic Society (ERS) and the Global Allergy and Asthma European Network (GA2LEN). One hundred and thirty participants (medical doctors from different specialties, researchers, as well as patients and industry representatives) from 27 countries took part in the multiple perspective discussions including brainstorming sessions on care pathways and research needs in rhinitis and rhinosinusitis.The debates started with an overview of the current state of the art, including weaknesses and strengths of the current practices, followed by the identification of essential research needs, thoroughly integrated in the context of Precision Medicine (PM), with personalized care, prediction of success of treatment, participation of the patient and prevention of disease as key principles for improving current clinical practices. This report provides a concise summary of the outcomes of the brainstorming sessions of the European Rhinology Research Forum 2016.

Published
2017

27. Conjunctival allergen provocation test : guidelines for daily practice

Author

Fauquert, J-L, Jedrzejczak-Czechowicz, M, Rondon, C, Calder, V, Silva, D, Kvenshagen, B K, Callebaut, I, Allegri, P, Santos, N, Doan, S, Perez Formigo, D, Chiambaretta, F, Delgado, L, Leonardi, A, and Interest Group on Ocular Allergy (IGOA) from the European Academy of Allergy and Clinical Immunology

Subjects
medicine.medical_specialty, Allergy, Exacerbation, allergen challenge, conjunctivitis, in vivo diagnosis, ocular surface, ocular surface diagnosis, provocation test, Immunology and Allergy, Immunology, Provocation test, medicine.disease_cause, 03 medical and health sciences, 0302 clinical medicine, Allergen, immune system diseases, otorhinolaryngologic diseases, Medicine, Humans, Asthma, Conjunctivitis, Allergic, Skin Tests, business.industry, Contraindications, Disease Management, Allergens, medicine.disease, Dermatology, Allergic conjunctivitis, respiratory tract diseases, 030228 respiratory system, Practice Guidelines as Topic, 030221 ophthalmology & optometry, Itching, medicine.symptom, business, Anaphylaxis
Abstract

Conjunctival allergen provocation test (CAPT) reproduces the events occurring by instilling an allergen on the ocular surface. This paper is the compilation of a task force focussed on practical aspects of this technique based on the analysis of 131 papers. Main mechanisms involved are reviewed. Indications are diagnosing the allergen(s)-triggering symptoms in IgE-mediated ocular allergy in seasonal, acute or perennial forms of allergic conjunctivitis, especially when the relevance of the allergen is not obvious or in polysensitized patients. Contraindications are limited to ongoing systemic severe pathology, asthma and eye diseases. CAPT should be delayed if receiving systemic steroids or antihistamines. Local treatment should be interrupted according to the half-life of each drug. Prerequisites are as follows: obtaining informed consent; evidencing of an allergen by skin prick tests and/or serum-specific IgE dosages; being able to deal with an unlikely event such as acute asthma exacerbation, urticaria or anaphylaxis, or an exacerbation of allergic conjunctivitis. Allergen extracts should be diluted locally prior to administration. Positive criteria are based on itching or quoted according to a composite score. An alternative scoring is based on itching. CAPT remains underused in daily practice, although it is a safe and simple procedure which can provide valuable clinical information.

Published
2016

30. Collaborative European neurotrauma effectiveness research in traumatic brain injury (CENTER-TBI): A prospective longitudinal observational study

Author

Maas, A.I.R. (Andrew), Menon, D.K. (David ), Steyerberg, E.W. (Ewout), Citerio, G. (Giuseppe), Lecky, F.E. (Fiona), Manley, G. (Geoffrey), Hill, S. (Sean), Legrand, V. (Valerie), Sorgner, A. (Annina), Andelic, N. (Nada), Andreassen, L. (Lasse), Andrews, P.J.D. (Peter), Audibert, G. (Gérard), Audny, A. (Anke), Azouv, P. (Philippe), Barzo, P. (P.), Beer, R. (Ronny), Bellander, B.-M. (Bo-Michael), Belli, A. (Antonio), Benali, H. (Habib), Berardino, M. (Maurizio), Beretta, L. (Luigi), Brazinova, A. (Alexandra), Binder, H. (Harald), Brehar, F. (Felix), Buki, A. (Andras), Bullinger, M. (Monika), Cakmak, E. (Ela), Callebaut, I. (Ina), Cameron, P. (Peter), Lozano, G.C. (Guillermo Carbayo), Carpenter, K.L.H. (Keri L.H.), Chieregato, A. (Arturo), Coburn, M. (Mark), Coles, J.P. (Jonathan P.), Cooper, J. (Jamie), Cnossen, M.C. (Maryse), Curry, N. (Nicola), Czeiter, E. (Endre), Czosnyka, M. (Marek), Dahyot-Fitzelier, C. (Claire), Damas, F. (François), Dawes, H. (Helen), De Keyser, V. (Véronique), De Luca, A. (Alessandra), De Ruiter, G.C.W. (Godard C.W.), De Witte, O. (Olivier), Corte, F.D. (Francesco), Demeter, B. (Béla), Depreitere, B. (Bart), Dippel, D.W.J. (Diederik), Dizdarevic, K. (Kemal), Dreier, J.P. (Jens), Eapen, G. (George), Ercole, A. (Ari), Esser, P. (Patrick), Fabricius, M. (Martin), Feremans, L. (Len), Feigin, V.L. (V.), Fossi, F. (Francesca), Forsyth, F. (Faye), Florian, S. (Stefan), Frisvold, S.K. (Shirin Kordasti), Frosini, C. (Caterina), Furmanov, A. (Alex), Frantzén, J. (Janek), Gadda, D. (Davide), Gagliardo, P. (Pablo), Galanaud, D. (Damien), Gao, G. (Guoyi), Ghuysen, A. (Alexandre), Godbolt, A. (Alison), Gonšorová, V. (Veronika), Grigore, Z. (Zapulih), Gruen, R.L. (Russell), Haagsma, J.A. (Juanita), Hallaert, G. (Giorgio), Hadzic, E. (Ermin), Haitsma, I. (Iain), Hartings, J.A. (Jed), Helbok, R. (Raimund), Helseth, E. (Eirik), Hoefer, S. (Stefan), Holling, M. (Markus), Hunfeld, M. (Maayke), Hutchinson, P.J. (Peter J.), Illéš, R. (Robert), Janssens, K. (Koen), Bovend'Eerdt, T.J.H. (Thamar J.H.), Jiang, J.-Y. (Ji-Yao), Jones, K.M. (Kelly M.), Kalala, J.-P. (Jean-Pierre), Kalovits, F. (Ferenc), Kasprian, G. (Gregor), Katila, A. (Ari), Ketharanathan, N. (Naomi), Kolias, A.G. (Angelos G.), Kolibay, F. (Felix), Kondziella, D. (Daniel), Koskinen, L.-O. (Lars-Owe), Lagares, A. (Alfonso), Lanyon, L. (Linda), Laureys, S. (Steven), Lefering, R., Levi, L. (Leon), Lightfoot, R. (Roger), Lingsma, H.F. (Hester), Loeckx, D. (Dirk), Lohkamp, L.-N. (Laura-Nanna), Lötjönen, J. (Jyrki), Lumenta, C. (Christianto), Lyttle, M.D. (Mark), Maegele, M. (Marc), Majdan, M. (Marek), Manara, A. (Alex), Maréchal, H. (Hugues), Martino, C. (Costanza), Mascia, L. (Luciana), Mauritz, W. (Walter), McMahon, C. (Catherine), Menovsky, T. (Tomas), Mitchell, P. (Patrick), Mladenov, N. (Nikolay), Morganti-Kossmann, C. (Cristina), Nelson, D. (David), Neugebauer, E. (Eddy), Newcombe, V.F. (Virginia F.), Oddo, M. (Mauro), Oresic, M. (Matej), Orzalesi, V. (Vanni), Outtrim, J.G. (Joanne G.), Palotie, A. (Aarno), Parizel, P.M., Payen, J.-F. (Jean-François), Perlbarg, V. (Vincent), Peul, W.C. (Wilco), Pichon, N. (Nicolas), Piippo, A. (Anna), Floury, S.P. (Sébastien Pili), Ples, H. (Horia), Polinder, S. (Suzanne), Preiksaitis, A. (Aidanas), Psota, M. (Marek), Pullens, P. (Pim), Puybasset, L. (Louis), Ragauskas, A. (Arminas), Raj, R. (Rahul), Reiner, M. (Michael), Rhodes, J.K.J. (Jonathan K.J.), Richardson, S. (Sylvia), Ripatti, S. (Samuli), Rocka, S. (Saulius), Roosenfeld, J. (Jeffrey), Rosand, J. (Jonathan), Rosenlund, C. (Christina), Rosenthal, G. (Guy), Rossaint, R. (Rolf), Rossi, S. (Sandra), Rueckert, D. (Daniel), Rusnák, M. (Martin), Rynkowski, M.A. (Michal A.), Sahuquillo, J. (Juan), Sakowitz, O. (Oliver), Sandor, J. (Janos), Schmidt, S. (Silke), Schoechl, H. (Herbert), Schou, R. (Rico), Skandsen, T. (Toril), Sonne, M. (Morten), Schwendenwein, E. (Elisabeth), Smeets, D. (Dirk), Smieleweski, P. (Peter), Söderberg, J. (Jeannette), Stamatakis, E. (Emmanuel), Stanworth, S. (Simon), Stefini, R. (Roberto), Stevens, R. (Robert), Stewart, W. (William), Stocchetti, N. (Nino), Stummer, W. (Walter), Szabó, J. (József), Tascu, A. (Alexandru), Tenovuo, O. (Olli), Theadom, A. (Alice), Tibboel, D. (Dick), Tolias, C.M. (Christos M.), Unterberg, A. (Andreas), Vajkoczy, P. (Peter), Vargiolu, A. (Alessia), Naalt, J. (Joukje) van der, Essen, T.A. (T.) van, Hecke, W. (Wim) van, Van Praag, D. (Dominique), Van Roost, D. (Dirk), Vandenbulcke, T. (Tim), Vande Hauwe, L. (Luc), Jagt, M. (Mathieu) van der, Vega, E. (Emmanuel), Verheyden, J. (Jan), Verma, V. (Vishwajit), Vespa, P.M. (Paul M.), Vik, A. (Anne), Vilcinis, R. (Rimantas), Von Steinbüchel, N. (Nicole), Vulekovic, P. (Peter), Wang, K.K.W. (Kevin), Wildschut, E. (Eno), Williams, G. (Guy), Wilson, M. (Mark), Wilson, L. (Lindsay), Wolf, S. (Stefan), Ylén, P. (Peter), Zaaroor, M. (Menashe), Zolfaghari, P. (Parjam), Martin, D. (Didier), D'Orio, V. (Vincenzo), Damas, P. (Pierre), Luaba Tshibanda, J.-F. (Jean-Flory), Maas, A.I.R. (Andrew), Menon, D.K. (David ), Steyerberg, E.W. (Ewout), Citerio, G. (Giuseppe), Lecky, F.E. (Fiona), Manley, G. (Geoffrey), Hill, S. (Sean), Legrand, V. (Valerie), Sorgner, A. (Annina), Andelic, N. (Nada), Andreassen, L. (Lasse), Andrews, P.J.D. (Peter), Audibert, G. (Gérard), Audny, A. (Anke), Azouv, P. (Philippe), Barzo, P. (P.), Beer, R. (Ronny), Bellander, B.-M. (Bo-Michael), Belli, A. (Antonio), Benali, H. (Habib), Berardino, M. (Maurizio), Beretta, L. (Luigi), Brazinova, A. (Alexandra), Binder, H. (Harald), Brehar, F. (Felix), Buki, A. (Andras), Bullinger, M. (Monika), Cakmak, E. (Ela), Callebaut, I. (Ina), Cameron, P. (Peter), Lozano, G.C. (Guillermo Carbayo), Carpenter, K.L.H. (Keri L.H.), Chieregato, A. (Arturo), Coburn, M. (Mark), Coles, J.P. (Jonathan P.), Cooper, J. (Jamie), Cnossen, M.C. (Maryse), Curry, N. (Nicola), Czeiter, E. (Endre), Czosnyka, M. (Marek), Dahyot-Fitzelier, C. (Claire), Damas, F. (François), Dawes, H. (Helen), De Keyser, V. (Véronique), De Luca, A. (Alessandra), De Ruiter, G.C.W. (Godard C.W.), De Witte, O. (Olivier), Corte, F.D. (Francesco), Demeter, B. (Béla), Depreitere, B. (Bart), Dippel, D.W.J. (Diederik), Dizdarevic, K. (Kemal), Dreier, J.P. (Jens), Eapen, G. (George), Ercole, A. (Ari), Esser, P. (Patrick), Fabricius, M. (Martin), Feremans, L. (Len), Feigin, V.L. (V.), Fossi, F. (Francesca), Forsyth, F. (Faye), Florian, S. (Stefan), Frisvold, S.K. (Shirin Kordasti), Frosini, C. (Caterina), Furmanov, A. (Alex), Frantzén, J. (Janek), Gadda, D. (Davide), Gagliardo, P. (Pablo), Galanaud, D. (Damien), Gao, G. (Guoyi), Ghuysen, A. (Alexandre), Godbolt, A. (Alison), Gonšorová, V. (Veronika), Grigore, Z. (Zapulih), Gruen, R.L. (Russell), Haagsma, J.A. (Juanita), Hallaert, G. (Giorgio), Hadzic, E. (Ermin), Haitsma, I. (Iain), Hartings, J.A. (Jed), Helbok, R. (Raimund), Helseth, E. (Eirik), Hoefer, S. (Stefan), Holling, M. (Markus), Hunfeld, M. (Maayke), Hutchinson, P.J. (Peter J.), Illéš, R. (Robert), Janssens, K. (Koen), Bovend'Eerdt, T.J.H. (Thamar J.H.), Jiang, J.-Y. (Ji-Yao), Jones, K.M. (Kelly M.), Kalala, J.-P. (Jean-Pierre), Kalovits, F. (Ferenc), Kasprian, G. (Gregor), Katila, A. (Ari), Ketharanathan, N. (Naomi), Kolias, A.G. (Angelos G.), Kolibay, F. (Felix), Kondziella, D. (Daniel), Koskinen, L.-O. (Lars-Owe), Lagares, A. (Alfonso), Lanyon, L. (Linda), Laureys, S. (Steven), Lefering, R., Levi, L. (Leon), Lightfoot, R. (Roger), Lingsma, H.F. (Hester), Loeckx, D. (Dirk), Lohkamp, L.-N. (Laura-Nanna), Lötjönen, J. (Jyrki), Lumenta, C. (Christianto), Lyttle, M.D. (Mark), Maegele, M. (Marc), Majdan, M. (Marek), Manara, A. (Alex), Maréchal, H. (Hugues), Martino, C. (Costanza), Mascia, L. (Luciana), Mauritz, W. (Walter), McMahon, C. (Catherine), Menovsky, T. (Tomas), Mitchell, P. (Patrick), Mladenov, N. (Nikolay), Morganti-Kossmann, C. (Cristina), Nelson, D. (David), Neugebauer, E. (Eddy), Newcombe, V.F. (Virginia F.), Oddo, M. (Mauro), Oresic, M. (Matej), Orzalesi, V. (Vanni), Outtrim, J.G. (Joanne G.), Palotie, A. (Aarno), Parizel, P.M., Payen, J.-F. (Jean-François), Perlbarg, V. (Vincent), Peul, W.C. (Wilco), Pichon, N. (Nicolas), Piippo, A. (Anna), Floury, S.P. (Sébastien Pili), Ples, H. (Horia), Polinder, S. (Suzanne), Preiksaitis, A. (Aidanas), Psota, M. (Marek), Pullens, P. (Pim), Puybasset, L. (Louis), Ragauskas, A. (Arminas), Raj, R. (Rahul), Reiner, M. (Michael), Rhodes, J.K.J. (Jonathan K.J.), Richardson, S. (Sylvia), Ripatti, S. (Samuli), Rocka, S. (Saulius), Roosenfeld, J. (Jeffrey), Rosand, J. (Jonathan), Rosenlund, C. (Christina), Rosenthal, G. (Guy), Rossaint, R. (Rolf), Rossi, S. (Sandra), Rueckert, D. (Daniel), Rusnák, M. (Martin), Rynkowski, M.A. (Michal A.), Sahuquillo, J. (Juan), Sakowitz, O. (Oliver), Sandor, J. (Janos), Schmidt, S. (Silke), Schoechl, H. (Herbert), Schou, R. (Rico), Skandsen, T. (Toril), Sonne, M. (Morten), Schwendenwein, E. (Elisabeth), Smeets, D. (Dirk), Smieleweski, P. (Peter), Söderberg, J. (Jeannette), Stamatakis, E. (Emmanuel), Stanworth, S. (Simon), Stefini, R. (Roberto), Stevens, R. (Robert), Stewart, W. (William), Stocchetti, N. (Nino), Stummer, W. (Walter), Szabó, J. (József), Tascu, A. (Alexandru), Tenovuo, O. (Olli), Theadom, A. (Alice), Tibboel, D. (Dick), Tolias, C.M. (Christos M.), Unterberg, A. (Andreas), Vajkoczy, P. (Peter), Vargiolu, A. (Alessia), Naalt, J. (Joukje) van der, Essen, T.A. (T.) van, Hecke, W. (Wim) van, Van Praag, D. (Dominique), Van Roost, D. (Dirk), Vandenbulcke, T. (Tim), Vande Hauwe, L. (Luc), Jagt, M. (Mathieu) van der, Vega, E. (Emmanuel), Verheyden, J. (Jan), Verma, V. (Vishwajit), Vespa, P.M. (Paul M.), Vik, A. (Anne), Vilcinis, R. (Rimantas), Von Steinbüchel, N. (Nicole), Vulekovic, P. (Peter), Wang, K.K.W. (Kevin), Wildschut, E. (Eno), Williams, G. (Guy), Wilson, M. (Mark), Wilson, L. (Lindsay), Wolf, S. (Stefan), Ylén, P. (Peter), Zaaroor, M. (Menashe), Zolfaghari, P. (Parjam), Martin, D. (Didier), D'Orio, V. (Vincenzo), Damas, P. (Pierre), and Luaba Tshibanda, J.-F. (Jean-Flory)

Abstract

BACKGROUND: Current classification of traumatic brain injury (TBI) is suboptimal, and management is based on weak evidence, with little attempt to personalize treatment. A need exists for new precision medicine and stratified management approaches that incorporate emerging technologies. OBJECTIVE: To improve characterization and classification of TBI and to identify best clinical care, using comparative effectiveness research approaches. METHODS: This multicenter, longitudinal, prospective, observational study in 22 countries across Europe and Israel will collect detailed data from 5400 consenting patients, presenting within 24 hours of injury, with a clinical diagnosis of TBI and an indication for computed tomography. Broader registry-level data collection in approximately 20 000 patients will assess generalizability. Cross sectional comprehensive outcome assessments, including quality of life and neuropsychological testing, will be performed at 6 months. Longitudinal assessments will continue up to 24 months post TBI in patient subsets. Advanced neuroimaging and genomic and biomarker data will be used to improve characterization, and analyses will include neuroinformatics approaches to address variations in process and clinical care. Results will be integrated with living systematic reviews in a process of knowledge transfer. The study initiation was from October to December 2014, and the recruitment period was for 18 to 24 months. EXPECTED OUTCOMES: Collaborative European NeuroTrauma Effectiveness Research in TBI should provide novel multidimensional approaches to TBI characterization and classification, evidence to support treatment recommendations, and benchmarks for quality of care. Data and sample repositories will ensure opportunities for legacy research. DISCUSSION: Comparative effectiveness research provides an alternative to reductionistic clinical trials in restricted patient populations by exploiting differences in biology, care, and outcome to support

Published
2015
Full Text
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31. Evolution of species-specific major seminal fluid proteins in placental mammals by gene death and positive selection

Author

Meslin, C., Laurin, M., Callebaut, I., Druart, X., Monget, P., Meslin, C., Laurin, M., Callebaut, I., Druart, X., and Monget, P.

Abstract

The seminal fluid is a complex substance composed of a variety of secreted proteins and has been shown to play an important role in the fertilisation process in mammals and also in Drosophila. Several genes under positive selection have been documented in some rodents and primates. Our study documents this phenomenon in several other mammalian taxa. We study the evolution of genes that encode for 20 proteins that are quantitatively predominant in the seminal fluid of at least one out of seven domestic animal species. We analyse the amino acid composition of these proteins for positive selection and for the presence of pseudogenes. Genes that disappeared through pseudogenisation include KLK2 in cattle, horse and mice. Traces of positive selection are found in seven genes. The identified amino acids are located in regions exposed to the protein surface, suggesting a role in the interaction of gametes, with possible impact on the process of speciation. Moreover, we found no evidence that the predominance of proteins in seminal fluid and their mode

Published
2015

32. The munc13-4–rab27 complex is specifically required for tethering secretory lysosomes at the plasma membrane

Author

Elstak, E.D.R., Neeft, M.A., Nehme, N.T., Voortman, J., Cheung, M., Goodarzifard, M., Gerritsen, H.C., van Bergen en Henegouwen, P.M.P., Callebaut, I., de Saint Basile, G., van der Sluijs, P., Celbiologie, Soft Condensed Matter and Biophysics, Dep Biologie, Sub Molecular Biophysics, and Sub Cell Biology

Abstract

Cytotoxic T lymphocytes (CTLs) kill target cells through the polarized release of lytic molecules from secretory lysosomes. Loss of munc13-4 function inhibits this process and causes familial hemophagocytic lymphohistiocytosis type 3 (FHL3). munc13-4 binds rab27a, but the necessity of the complex remains enigmatic, because studies in knockout models suggest separate functions. In the present study, we describe a noncanonical rab27abinding motif in the N-terminus of munc13-4. Point mutants in this sequence have severely impaired rab27a binding, allowing dissection of rab27a requirements in munc13-4 function. The munc13- 4–rab27a complex is not needed for secretory lysosome maturation, as shown by complementation in CTLs from FHL3 patients and in a mast cell line silenced for munc13-4. In contrast, fusion of secretory lysosomes with, and content release at the plasma membrane during degranulation, strictly required the munc13-4– rab27a complex. Total internal reflection fluorescence microscopy imaging revealed that the complex corrals motile secretory lysosomes beneath the plasma membrane during degranulation and controls their docking. The propensity to stall motility of secretory lysosomes is lost in cells expressing munc13-4 point mutants that do not bind rab27. In summary, these results uncovered a mechanism for tethering secretory lysosomes to the plasma membrane that is essential for degranulation in immune cells.

Published
2011

33. OCRE: a novel domain made of imperfect, aromatic-rich octamer repeats

Author

Callebaut, I., Mornon, J.P., Institut de minéralogie et de physique des milieux condensés (IMPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Physique du Globe de Paris (IPG Paris)-Centre National de la Recherche Scientifique (CNRS)

Subjects
GENES, IDENTIFICATION, DATABASE, CELLS, MOTIF, 3P21.3, PATTERNS, RNA-BINDING PROTEIN, PUTATIVE TUMOR-SUPPRESSOR, REGION
Abstract

In this study, we describe a novel domain, OCRE, which is shared by the recently identified angiogenic factor VG5Q and a specific family of RNA-binding motif proteins. The OCRE domain is characterized by a 5-fold, imperfectly repeated octameric sequence, which includes a triplet of often-conserved aromatic amino acids predicted to form a beta-strand and in which the slightly modified fifth repeat might act as a repeat terminator. Although the function of this domain remains to be elucidated, the domain architecture of OCRE containing proteins and experimental data suggest a role in RNA metabolism and/or in signalling pathways activated by the tumor necrosis factor superfamily of cytokines.

Published
2005

34. Identification of the hydrophobic strand in the A-B loop of leptin as a major binding site III: implications for large-scale preparation of potent recombinant human and ovine leptin antagonists

Author

Niv-Spector, L., Gonen-Berger, D., Gourdou, Isabelle, Biener, E., Gussakovsky, E.E., Benomar, Yacir, Ramanujan, K.V., Taouis, Mohammed, Herman, B., Callebaut, I., Djiane, Jean, Gertler, A., Neurobiologie de l'Olfaction et de la Prise Alimentaire (NOPA), and Institut National de la Recherche Agronomique (INRA)

Subjects
STRUCTURE, [SDV]Life Sciences [q-bio], [INFO]Computer Science [cs], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2005

36. Comprehensive functional annotation of 18 missense mutations found in suspected hemochromatosis type 4 patients

Author

Callebaut, I., primary, Joubrel, R., additional, Pissard, S., additional, Kannengiesser, C., additional, Gerolami, V., additional, Ged, C., additional, Cadet, E., additional, Cartault, F., additional, Ka, C., additional, Gourlaouen, I., additional, Gourhant, L., additional, Oudin, C., additional, Goossens, M., additional, Grandchamp, B., additional, De Verneuil, H., additional, Rochette, J., additional, Ferec, C., additional, and Le Gac, G., additional

Published
2014
Full Text
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37. Mutation in bone morphogenetic protein receptor-IB is associated with increased ovulation rate in Booroola Mérino ewes

Author

Mulsant, Philippe, Lecerf, Frédéric, Fabre, Stéphane, Schibler, Laurent, Monget, Philippe, Lanneluc, I., Pisselet, C., Riquet, Juliette, Monniaux, Danielle, Callebaut, I., Cribiu, Edmond, Thimonier, Jacques, Teyssier, Jacques, Bodin, Loys, Chitour, N., Elsen, Jean Michel, Laboratoire de Génétique Cellulaire (LGC), Institut National de la Recherche Agronomique (INRA)-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS), Unité de recherche Génétique Biochimique et Cytogénétique (LGBC), Institut National de la Recherche Agronomique (INRA), Elevage des ruminants en régions chaudes (UMR ERRC), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA), Station d'Amélioration Génétique des Animaux (SAGA), and Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV]Life Sciences [q-bio], [INFO]Computer Science [cs], GENETIQUE, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2001

38. The munc13-4–rab27 complex is specifically required for tethering secretory lysosomes at the plasma membrane

Author

Celbiologie, Soft Condensed Matter and Biophysics, Dep Biologie, Sub Molecular Biophysics, Sub Cell Biology, Elstak, E.D.R., Neeft, M.A., Nehme, N.T., Voortman, J., Cheung, M., Goodarzifard, M., Gerritsen, H.C., van Bergen en Henegouwen, P.M.P., Callebaut, I., de Saint Basile, G., van der Sluijs, P., Celbiologie, Soft Condensed Matter and Biophysics, Dep Biologie, Sub Molecular Biophysics, Sub Cell Biology, Elstak, E.D.R., Neeft, M.A., Nehme, N.T., Voortman, J., Cheung, M., Goodarzifard, M., Gerritsen, H.C., van Bergen en Henegouwen, P.M.P., Callebaut, I., de Saint Basile, G., and van der Sluijs, P.

Published
2011

39. The munc13-4–rab27 complex is specifically required for tethering secretory lysosomes at the plasma membrane

Author

Cell Biology, Neurobiology and Biophysics, Soft Condensed Matter and Biophysics, Dep Biologie, Sub Molecular Biophysics, Sub Cell Biology, Elstak, E.D.R., Neeft, M.A., Nehme, N.T., Voortman, J., Cheung, M., Goodarzifard, M., Gerritsen, H.C., van Bergen en Henegouwen, P.M.P., Callebaut, I., de Saint Basile, G., van der Sluijs, P., Cell Biology, Neurobiology and Biophysics, Soft Condensed Matter and Biophysics, Dep Biologie, Sub Molecular Biophysics, Sub Cell Biology, Elstak, E.D.R., Neeft, M.A., Nehme, N.T., Voortman, J., Cheung, M., Goodarzifard, M., Gerritsen, H.C., van Bergen en Henegouwen, P.M.P., Callebaut, I., de Saint Basile, G., and van der Sluijs, P.

Published
2011

40. Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction

Author

Girault, J. A., Labesse, G., Mornon, J. P., and Callebaut, I.

Subjects
Molecular Sequence Data, Neuropeptides, Membrane Proteins, macromolecular substances, Protein-Tyrosine Kinases, Cytoskeletal Proteins, Focal Adhesion Kinase 1, Focal Adhesion Protein-Tyrosine Kinases, Animals, Humans, Amino Acid Sequence, Cell Adhesion Molecules, Phylogeny, Research Article, Signal Transduction
Abstract

The band 4.1 domain was first identified in the red blood cell protein band 4.1, and subsequently in ezrin, radixin, and moesin (ERM proteins) and other proteins, including tumor suppressor merlin/schwannomin, talin, unconventional myosins VIIa and X, and protein tyrosine phosphatases. Recently, the presence of a structurally related domain has been demonstrated in the N-terminal region of two groups of tyrosine kinases: the focal adhesion kinases (FAK) and the Janus kinases (JAK). Additional proteins containing the 4.1/JEF (JAK, ERM, FAK) domain include plant kinesin-like calmodulin-binding proteins (KCBP) and a number of uncharacterized open reading frames identified by systematic DNA sequencing. Phylogenetic analysis of amino acid sequences suggests that band 4.1/JEF domains can be grouped in several families that have probably diverged early during evolution. Hydrophobic cluster analysis indicates that the band 4.1/JEF domains might consist of a duplicated module of approximately 140 residues and a central hinge region. A conserved property of the domain is its capacity to bind to the membrane-proximal region of the C-terminal cytoplasmic tail of proteins with a single transmembrane segment. Many proteins with band 4.1/JEF domains undergo regulated intra- or intermolecular homotypic interactions. Additional properties common to band 4.1/JEF domains of several proteins are binding of phosphoinositides and regulation by GTPases of the Rho family. Many proteins with band 4. 1/JEF domains are associated with the actin-based cytoskeleton and are enriched at points of contact with other cells or the extracellular matrix, from which they can exert control over cell growth. Thus, proteins with band 4.1/JEF domain are at the crossroads between cytoskeletal organization and signal transduction in multicellular organisms. Their importance is underlined by the variety of diseases that can result from their mutations.

Published
1998

42. Active-site motifs of lysosomal acid hydrolases: invariant features of clan GH-A of glycosyl hydrolases deduced from hydrophobic cluster analysis

Author

Durand, P., Lehn, P., Callebaut, I., Fabrega, S., Henrissat, Bernard, Mornon, J.P., Centre de Recherches sur les Macromolécules Végétales (CERMAV), and Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)

Subjects
ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
1997

43. Functional analysis of the NUP98-CCDC28A fusion protein

Author

Petit, A., primary, Ragu, C., additional, Soler, G., additional, Ottolenghi, C., additional, Schluth, C., additional, Radford-Weiss, I., additional, Schneider-Maunoury, S., additional, Callebaut, I., additional, Dastugue, N., additional, Drabkin, H. A., additional, Bernard, O. A., additional, Romana, S., additional, and Penard-Lacronique, V., additional

Published
2011
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