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146 results on '"Altelaar, A.F."'

2. Feedback-Driven Assembly of the Axon Initial Segment

Author

Fréal, Amélie, Rai, Dipti, Tas, Roderick P., Pan, Xingxiu, Katrukha, Eugene A., van de Willige, Dieudonnée, Stucchi, Riccardo, Aher, Amol, Yang, Chao, Altelaar, A.F. Maarten, Vocking, Karin, Post, Jan Andries, Harterink, Martin, Kapitein, Lukas C., Akhmanova, Anna, and Hoogenraad, Casper C.

Published
2019
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5. Maternal allergic sensitization affects the T cell modulatory capacity and molecular cargo of milk derived extracellular vesicles

Author

van Herwijnen, Martijn J. C., primary, Giovanazzi, Alberta, additional, Zonneveld, Marijke I., additional, Maqueda, Joaquin J., additional, Kleinjan, Marije, additional, Goerdayal, Soenita, additional, Vollmy, Franziska, additional, van Bruggen - de Haan, Arianne, additional, Driedonks, Tom A.P., additional, Arkesteijn, Ger J.A., additional, van Elburg, Ruurd M., additional, van der Meulen, Gerbrich N., additional, Garssen, Johan, additional, Oliveira, Carla, additional, Altelaar, A.F. Maarten, additional, 't Hoen, Peter A.C., additional, Redegeld, Frank A., additional, Nolte- 't Hoen, Esther N.M., additional, and Wauben, Marca H.M., additional

Published
2023
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8. BRAFV600E Kinase Domain Duplication Identified in Therapy-Refractory Melanoma Patient-Derived Xenografts

Author

Kemper, Kristel, Krijgsman, Oscar, Kong, Xiangjun, Cornelissen-Steijger, Paulien, Shahrabi, Aida, Weeber, Fleur, van der Velden, Daphne L., Bleijerveld, Onno B., Kuilman, Thomas, Kluin, Roel J.C., Sun, Chong, Voest, Emile E., Ju, Young Seok, Schumacher, Ton N.M., Altelaar, A.F. Maarten, McDermott, Ultan, Adams, David J., Blank, Christian U., Haanen, John B., and Peeper, Daniel S.

Published
2016
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10. Table S6A from Membrane-Depolarizing Channel Blockers Induce Selective Glioma Cell Death by Impairing Nutrient Transport and Unfolded Protein/Amino Acid Responses

Author

Niklasson, Mia, primary, Maddalo, Gianluca, primary, Sramkova, Zuzana, primary, Mutlu, Ercan, primary, Wee, Shimei, primary, Sekyrova, Petra, primary, Schmidt, Linnéa, primary, Fritz, Nicolas, primary, Dehnisch, Ivar, primary, Kyriatzis, Gregorios, primary, Krafcikova, Michaela, primary, Carson, Brittany B., primary, Feenstra, Jennifer M., primary, Marinescu, Voichita D., primary, Segerman, Anna, primary, Haraldsson, Martin, primary, Gustavsson, Anna-Lena, primary, Hammarström, Lars G.J., primary, Jenmalm Jensen, Annika, primary, Uhrbom, Lene, primary, Altelaar, A.F. Maarten, primary, Linnarsson, Sten, primary, Uhlén, Per, primary, Trantirek, Lukas, primary, Vincent, C. Theresa, primary, Nelander, Sven, primary, Enger, Per Øyvind, primary, and Andäng, Michael, primary

Published
2023
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11. Figure S4 from Membrane-Depolarizing Channel Blockers Induce Selective Glioma Cell Death by Impairing Nutrient Transport and Unfolded Protein/Amino Acid Responses

Author

Niklasson, Mia, primary, Maddalo, Gianluca, primary, Sramkova, Zuzana, primary, Mutlu, Ercan, primary, Wee, Shimei, primary, Sekyrova, Petra, primary, Schmidt, Linnéa, primary, Fritz, Nicolas, primary, Dehnisch, Ivar, primary, Kyriatzis, Gregorios, primary, Krafcikova, Michaela, primary, Carson, Brittany B., primary, Feenstra, Jennifer M., primary, Marinescu, Voichita D., primary, Segerman, Anna, primary, Haraldsson, Martin, primary, Gustavsson, Anna-Lena, primary, Hammarström, Lars G.J., primary, Jenmalm Jensen, Annika, primary, Uhrbom, Lene, primary, Altelaar, A.F. Maarten, primary, Linnarsson, Sten, primary, Uhlén, Per, primary, Trantirek, Lukas, primary, Vincent, C. Theresa, primary, Nelander, Sven, primary, Enger, Per Øyvind, primary, and Andäng, Michael, primary

Published
2023
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12. Supplementary Information from Membrane-Depolarizing Channel Blockers Induce Selective Glioma Cell Death by Impairing Nutrient Transport and Unfolded Protein/Amino Acid Responses

Author

Niklasson, Mia, primary, Maddalo, Gianluca, primary, Sramkova, Zuzana, primary, Mutlu, Ercan, primary, Wee, Shimei, primary, Sekyrova, Petra, primary, Schmidt, Linnéa, primary, Fritz, Nicolas, primary, Dehnisch, Ivar, primary, Kyriatzis, Gregorios, primary, Krafcikova, Michaela, primary, Carson, Brittany B., primary, Feenstra, Jennifer M., primary, Marinescu, Voichita D., primary, Segerman, Anna, primary, Haraldsson, Martin, primary, Gustavsson, Anna-Lena, primary, Hammarström, Lars G.J., primary, Jenmalm Jensen, Annika, primary, Uhrbom, Lene, primary, Altelaar, A.F. Maarten, primary, Linnarsson, Sten, primary, Uhlén, Per, primary, Trantirek, Lukas, primary, Vincent, C. Theresa, primary, Nelander, Sven, primary, Enger, Per Øyvind, primary, and Andäng, Michael, primary

Published
2023
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13. Data from Membrane-Depolarizing Channel Blockers Induce Selective Glioma Cell Death by Impairing Nutrient Transport and Unfolded Protein/Amino Acid Responses

Author

Niklasson, Mia, primary, Maddalo, Gianluca, primary, Sramkova, Zuzana, primary, Mutlu, Ercan, primary, Wee, Shimei, primary, Sekyrova, Petra, primary, Schmidt, Linnéa, primary, Fritz, Nicolas, primary, Dehnisch, Ivar, primary, Kyriatzis, Gregorios, primary, Krafcikova, Michaela, primary, Carson, Brittany B., primary, Feenstra, Jennifer M., primary, Marinescu, Voichita D., primary, Segerman, Anna, primary, Haraldsson, Martin, primary, Gustavsson, Anna-Lena, primary, Hammarström, Lars G.J., primary, Jenmalm Jensen, Annika, primary, Uhrbom, Lene, primary, Altelaar, A.F. Maarten, primary, Linnarsson, Sten, primary, Uhlén, Per, primary, Trantirek, Lukas, primary, Vincent, C. Theresa, primary, Nelander, Sven, primary, Enger, Per Øyvind, primary, and Andäng, Michael, primary

Published
2023
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14. TRIM46 Controls Neuronal Polarity and Axon Specification by Driving the Formation of Parallel Microtubule Arrays

Author

van Beuningen, Sam F.B., Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y., Frias, Cátia P., Franker, Mariella A.M., Katrukha, Eugene A., Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T., Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A.F. Maarten, Post, Jan A., Akhmanova, Anna, Pasterkamp, R. Jeroen, Kapitein, Lukas C., de Graaff, Esther, and Hoogenraad, Casper C.

Published
2015
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26. A central role for TFIID in the pluripotent transcription circuitry

Author

Pijnappel, W.W.M. Pim, Esch, Daniel, Baltissen, Marijke P.A., Wu, Guangming, Mischerikow, Nikolai, Bergsma, Atze J., van der Wal, Erik, Han, Dong Wook, Bruch, Hermann vom, Moritz, Soren, Lijnzaad, Phillip, Altelaar, A.F. Maarten, Sameith, Katrin, Zaehres, Holm, Heck, Albert J.R., Holstege, Frank C.P., Scholer, Hans R., and Timmers, H.T. Marc

Subjects
Gene expression -- Testing, Embryonic stem cells -- Research, Cellular control mechanisms -- Testing, Transcription factors -- Properties, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Embryonic stem (ES) cells are pluripotent and characterized by open chromatin and high transcription levels, achieved through auto-regulatory and feed-forward transcription factor loops (1,2). ES-cell identity is maintained by a [...]

Published
2013

30. Gold-enhanced biomolecular surface imaging of cells and tissue by SIMS and MALDI mass spectrometry

Author

Altelaar, A.F. Maarten, Klinkert, Ivo, Jalink, Kees, Lange, Robert P.J. de, Adan, Roger A.H., Heeren, Ron M.A., and Piersma, Sander R.

Subjects
Mass spectrometry -- Analysis, Biomolecules -- Optical properties, Ionization -- Analysis, Chemistry
Abstract

Surface metallization by plasma coating enhances desorption/ionization of membrane components such as lipids and sterols in imaging time-of-flight secondary ion mass spectrometry (TOF-SIMS) of tissues and cells. High-resolution images of cholesterol and other membrane components were obtained for neuroblastoma cells and revealed subcellular details (resolving power 1.5 [micro]m). Alternatively, in matrix-enhanced SIMS, 2,5-dihydroxybenzoic acid electrosprayed on neuroblastoma cells allowed intact molecular ion imaging of phosphatidylcholine and sphingomyelin at the cellular level. Gold deposition on top of matrix-coated rat brain tissue sections strongly enhanced image quality and signal intensity in stigmatic matrix-assisted laser desorption/ionization imaging mass spectrometry. High-quality total ion count images were acquired, and the neuropeptide vasopressin was localized in the rat brain tissue section at the hypothalamic area around the third ventricle. Although the mechanism of signal enhancement by gold deposition is under debate, the results we have obtained for cells and tissue sections illustrate the potential of this sample preparation technique for biomolecular surface imaging by mass spectrometry.

Published
2006

31. Direct molecular imaging of Lymnaea stagnalis nervous tissue at subcellular spatial resolution by mass spectrometry

Author

Altelaar, A.F. Maarten, van Minnen, Jan, Jimenez, Connie R., Heeren, Ron M.A., and Piersma, Sander R.

Subjects
Mass spectrometry -- Research, Chemistry
Abstract

The imaging capabilities of time-of-flight secondary ion mass spectrometry (ToF-SIMS) and MALDI-MS sample preparation methods were combined. We used this method, named matrix-enhanced (ME) SIMS, for direct molecular imaging of nervous tissue at micrometer spatial resolution. Cryosections of the cerebral ganglia of the freshwater snail Lymnaea stagnalis were placed on indium-tin-oxide (ITO)-coated conductive glass slides and covered with a thin layer of 2,5-dihydroxybenzoic acid by electrospray deposition. High-resolution molecular ion maps of cholesterol and the neuropeptide APGWamide were constructed. APGWamide was predominantly localized in the cluster of neurons that regulate male copulation behavior of Lymnaea. ME-SIMS imaging allows direct molecule-specific imaging from tissue sections without labeling and opens a complementary mass window (

Published
2005

34. MAP7 family proteins regulate kinesin-1 recruitment and activation

Author

Hooikaas, Peter Jan, primary, Martin, Maud, additional, Mühlethaler, Tobias, additional, Kuijntjes, Gert-Jan, additional, Peeters, Cathelijn A.E., additional, Katrukha, Eugene A., additional, Ferrari, Luca, additional, Stucchi, Riccardo, additional, Verhagen, Daan G.F., additional, van Riel, Wilhelmina E., additional, Grigoriev, Ilya, additional, Altelaar, A.F. Maarten, additional, Hoogenraad, Casper C., additional, Rüdiger, Stefan G.D., additional, Steinmetz, Michel O., additional, Kapitein, Lukas C., additional, and Akhmanova, Anna, additional

Published
2019
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35. Evolutionarily-conserved chromatin crosstalk generates a DOT1L-dose dependency in thymic lymphoma caused by loss of HDAC1

Author

Vlaming, Hanneke, primary, McLean, Chelsea M., additional, Korthout, Tessy, additional, Alemdehy, Mir Farshid, additional, Hendriks, Sjoerd, additional, Lancini, Cesare, additional, Palit, Sander, additional, Klarenbeek, Sjoerd, additional, Kwesi-Maliepaard, Eliza Mari, additional, Molenaar, Thom M., additional, Hoekman, Liesbeth, additional, Schmidlin, Thierry T., additional, Altelaar, A.F. Maarten, additional, van Welsem, Tibor, additional, Dannenberg, Jan-Hermen, additional, Jacobs, Heinz, additional, and Leeuwen, Fred van, additional

Published
2019
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36. Opposite Electron-Transfer Dissociation and Higher-Energy Collisional Dissociation Fragmentation Characteristics of Proteolytic K/R(X)n and (X)nK/R Peptides Provide Benefits for Peptide Sequencing in Proteomics and Phosphoproteomics

Author

Tsiatsiani, Liana, Giansanti, Piero, Scheltema, Richard A., van den Toorn, Henk, Overall, Christopher M., Altelaar, A.F. Maarten, Heck, Albert J.R., Sub Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., and Biomolecular Mass Spectrometry and Proteomics

Subjects
trypsin, peptide fragmentation, LysargiNase, proteomics, higher-energy collisional dissociation, Taverne, phosphoproteomics, electron-transfer dissociation
Abstract

A key step in shotgun proteomics is the digestion of proteins into peptides amenable for mass spectrometry. Tryptic peptides can be readily sequenced and identified by collision-induced dissociation (CID) or higher-energy collisional dissociation (HCD) because the fragmentation rules are well-understood. Here, we investigate LysargiNase, a perfect trypsin mirror protease, because it cleaves equally specific at arginine and lysine residues, albeit at the N-terminal end. LysargiNase peptides are therefore practically tryptic-like in length and sequence except that following ESI, the two protons are now both positioned at the N-terminus. Here, we compare side-by-side the chromatographic separation properties, gas-phase fragmentation characteristics, and (phospho)proteome sequence coverage of tryptic (i.e., (X)nK/R) and LysargiNase (i.e., K/R(X)n) peptides using primarily electron-transfer dissociation (ETD) and, for comparison, HCD. We find that tryptic and LysargiNase peptides fragment nearly as mirror images. For LysargiNase predominantly N-terminal peptide ions (c-ions (ETD) and b-ions (HCD)) are formed, whereas for trypsin, C-terminal fragment ions dominate (z-ions (ETD) and y-ions (HCD)) in a homologous mixture of complementary ions. Especially during ETD, LysargiNase peptides fragment into low-complexity but information-rich sequence ladders. Trypsin and LysargiNase chart distinct parts of the proteome, and therefore, the combined use of these enzymes will benefit a more in-depth and reliable analysis of (phospho)proteomes.

Published
2017

37. Identification of Putative Substrates for the Periplasmic Chaperone YfgM inEscherichia coliUsing Quantitative Proteomics

Author

Götzke, Hansjörg, Muheim, Claudio, Altelaar, A.F. Maarten, Heck, Albert J.R., Maddalo, Gianluca, Daley, Daniel O., Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spect. and Proteomics, and Sub Biomol.Mass Spectrometry & Proteom.

Subjects
Proteomics, protein CusS, periplasmic protein, protein WrbA, Biochemistry, Analytical Chemistry, protein folding, protein YcgK, chaperone, membrane protein, protein AnsB, protein Ggt, quantitative analysis, biology, Escherichia coli Proteins, lipoprotein, article, unclassified drug, protein metabolism, protein YnjE, protein degradation, Protein folding, bacterial gene, Bacterial outer membrane, protein HdeA, protein HdeB, Quantitative proteomics, protein YtfH, protein MalF, Protein degradation, protein MalE, Escherichia coli protein, outer membrane protein, loss of function mutation, tandem mass spectrometry, Escherichia coli, liquid chromatography, Inner membrane, controlled study, protein YfgM, protein expression, Molecular Biology, inner membrane, protein OsmC, nonhuman, Research, Membrane Proteins, Periplasmic space, asparaginase, bacterial strain, protein YfhB, structural proteomics, envelope protein, Membrane protein, protein TdcB, protein analysis, Chaperone (protein), protein TdcC, biology.protein, protein EvgS, Molecular Chaperones
Abstract

How proteins are trafficked, folded, and assembled into functional units in the cell envelope of Gram-negative bacteria is of significant interest. A number of chaperones have been identified, however, the molecular roles of these chaperones are often enigmatic because it has been challenging to assign substrates. Recently we discovered a novel periplasmic chaperone, called YfgM, which associates with PpiD and the SecYEG translocon and operates in a network that contains Skp and SurA. The aim of the study presented here was to identify putative substrates of YfgM. We reasoned that substrates would be incorrectly folded or trafficked when YfgM was absent from the cell, and thus more prone to proteolysis (the loss-of-function rationale). We therefore used a comparative proteomic approach to identify cell envelope proteins that were lower in abundance in a strain lacking yfgM, and strains lacking yfgM together with either skp or surA. Sixteen putative substrates were identified. The list contained nine inner membrane proteins (CusS, EvgS, MalF, OsmC, TdcB, TdcC, WrbA, YfhB, and YtfH) and seven periplasmic proteins (HdeA, HdeB, AnsB, Ggt, MalE, YcgK, and YnjE), but it did not include any lipoproteins or outer membrane proteins. Significantly, AnsB (an asparaginase) and HdeB (a protein involved in the acid stress response), were lower in abundance in all three strains lacking yfgM. For both genes, we ruled out the possibility that they were transcriptionally down-regulated, so it is highly likely that the corresponding proteins are misfolded/mistargeted and turned-over in the absence of YfgM. For HdeB we validated this conclusion in a pulse-chase experiment. The identification of HdeB and other cell envelope proteins as potential substrates will be a valuable resource for follow-up experiments that aim to delineate molecular the function of YfgM.

Published
2014
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38. MAP7 family proteins regulate kinesin-1 recruitment and activation

Author

Hooikaas, Peter Jan, primary, Martin, Maud, additional, Mühlethaler, Tobias, additional, Kuijntjes, Gert-Jan, additional, Peeters, Cathelijn A.E., additional, Katrukha, Eugene A., additional, Ferrari, Luca, additional, Stucchi, Riccardo, additional, Verhagen, Daan G.F., additional, Riel, Wilhelmina E. van, additional, Grigoriev, Ilya, additional, Altelaar, A.F. Maarten, additional, Hoogenraad, Casper C., additional, Rüdiger, Stefan G.D., additional, Steinmetz, Michel O., additional, Kapitein, Lukas C., additional, and Akhmanova, Anna, additional

Published
2018
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39. A system-wide approach to monitor responses to synergistic BRAF and EGFR inhibition in colorectal cancer cells

Author

Ressa, Anna, primary, Bosdriesz, Evert, additional, de Ligt, Joep, additional, Mainardi, Sara, additional, Maddalo, Gianluca, additional, Prahallad, Anirudh, additional, Jager, Myrthe, additional, de la Fonteijne, Lisanne, additional, Fitzpatrick, Martin, additional, Groten, Stijn, additional, Altelaar, A.F. Maarten, additional, Bernards, Renn, additional, Cuppen, Edwin, additional, Wessels, Lodewyk, additional, and Heck, Albert J.R., additional

Published
2018
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40. High-Throughput Assessment of Kinome-Wide Activation States

Author

Schmidlin, Thierry, primary, Rontogianni, Stamatia, additional, van Gelder, Charlotte A. G. H., additional, Stecker, Kelly E., additional, Eshof, Bart L. van den, additional, Kemper, Kristel, additional, Lips, Esther H., additional, Biggelaar, Maartje van den, additional, Peeper, Daniel S., additional, Heck, Albert J. R., additional, and Altelaar, A.F. Maarten, additional

Published
2018
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41. Opposite Electron-Transfer Dissociation and Higher-Energy Collisional Dissociation Fragmentation Characteristics of Proteolytic K/R(X)n and (X)nK/R Peptides Provide Benefits for Peptide Sequencing in Proteomics and Phosphoproteomics

Author

Sub Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Tsiatsiani, Liana, Giansanti, Piero, Scheltema, Richard A., van den Toorn, Henk, Overall, Christopher M., Altelaar, A.F. Maarten, Heck, Albert J.R., Sub Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Tsiatsiani, Liana, Giansanti, Piero, Scheltema, Richard A., van den Toorn, Henk, Overall, Christopher M., Altelaar, A.F. Maarten, and Heck, Albert J.R.

Published
2017

42. Membrane-Depolarizing Channel Blockers Induce Selective Glioma Cell Death by Impairing Nutrient Transport and Unfolded Protein/Amino Acid Responses

Author

Niklasson, Mia, primary, Maddalo, Gianluca, additional, Sramkova, Zuzana, additional, Mutlu, Ercan, additional, Wee, Shimei, additional, Sekyrova, Petra, additional, Schmidt, Linnéa, additional, Fritz, Nicolas, additional, Dehnisch, Ivar, additional, Kyriatzis, Gregorios, additional, Krafcikova, Michaela, additional, Carson, Brittany B., additional, Feenstra, Jennifer M., additional, Marinescu, Voichita D., additional, Segerman, Anna, additional, Haraldsson, Martin, additional, Gustavsson, Anna-Lena, additional, Hammarström, Lars G.J., additional, Jenmalm Jensen, Annika, additional, Uhrbom, Lene, additional, Altelaar, A.F. Maarten, additional, Linnarsson, Sten, additional, Uhlén, Per, additional, Trantirek, Lukas, additional, Vincent, C. Theresa, additional, Nelander, Sven, additional, Enger, Per Øyvind, additional, and Andäng, Michael, additional

Published
2017
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44. Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics

Author

Götzke, Hansjörg, Muheim, Claudio, Altelaar, A.F. Maarten, Heck, Albert J.R., Maddalo, Gianluca, Daley, Daniel O., Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spect. and Proteomics, and Sub Biomol.Mass Spectrometry & Proteom.

Subjects
protein CusS, protein HdeA, periplasmic protein, protein HdeB, protein WrbA, protein YtfH, protein MalF, protein MalE, Escherichia coli protein, outer membrane protein, loss of function mutation, protein folding, tandem mass spectrometry, protein YcgK, Escherichia coli, chaperone, liquid chromatography, membrane protein, controlled study, protein YfgM, protein AnsB, protein expression, inner membrane, protein OsmC, nonhuman, protein Ggt, quantitative analysis, lipoprotein, article, asparaginase, bacterial strain, protein YfhB, unclassified drug, structural proteomics, envelope protein, protein TdcB, protein analysis, protein metabolism, protein YnjE, protein TdcC, protein degradation, protein EvgS, bacterial gene
Abstract

How proteins are trafficked, folded, and assembled into functional units in the cell envelope of Gram-negative bacteria is of significant interest. A number of chaperones have been identified, however, the molecular roles of these chaperones are often enigmatic because it has been challenging to assign substrates. Recently we discovered a novel periplasmic chaperone, called YfgM, which associates with PpiD and the SecYEG translocon and operates in a network that contains Skp and SurA. The aim of the study presented here was to identify putative substrates of YfgM. We reasoned that substrates would be incorrectly folded or trafficked when YfgM was absent from the cell, and thus more prone to proteolysis (the loss-of-function rationale). We therefore used a comparative proteomic approach to identify cell envelope proteins that were lower in abundance in a strain lacking yfgM, and strains lacking yfgM together with either skp or surA. Sixteen putative substrates were identified. The list contained nine inner membrane proteins (CusS, EvgS, MalF, OsmC, TdcB, TdcC, WrbA, YfhB, and YtfH) and seven periplasmic proteins (HdeA, HdeB, AnsB, Ggt, MalE, YcgK, and YnjE), but it did not include any lipoproteins or outer membrane proteins. Significantly, AnsB (an asparaginase) and HdeB (a protein involved in the acid stress response), were lower in abundance in all three strains lacking yfgM. For both genes, we ruled out the possibility that they were transcriptionally down-regulated, so it is highly likely that the corresponding proteins are misfolded/mistargeted and turned-over in the absence of YfgM. For HdeB we validated this conclusion in a pulse-chase experiment. The identification of HdeB and other cell envelope proteins as potential substrates will be a valuable resource for follow-up experiments that aim to delineate molecular the function of YfgM.

Published
2015

45. Talin-KANK1 interaction controls the recruitment of cortical microtubule stabilizing complexes to focal adhesions

Author

Bouchet, Benjamin P., Gough, Rosemarie E., Ammon, York-Christoph, van de Willige, Dieudonnee, Post, Harm, Jacquemet, Guillaume, Altelaar, A.F. Maarten, Heck, Albert J.R., Goult, Benjamin T., Akhmanova, Anna, Bouchet, Benjamin P., Gough, Rosemarie E., Ammon, York-Christoph, van de Willige, Dieudonnee, Post, Harm, Jacquemet, Guillaume, Altelaar, A.F. Maarten, Heck, Albert J.R., Goult, Benjamin T., and Akhmanova, Anna

Abstract

The cross-talk between dynamic microtubules and integrin-based adhesions to the extracellular matrix plays a crucial role in cell polarity and migration. Microtubules regulate the turnover of adhesion sites, and, in turn, focal adhesions promote cortical microtubule capture and stabilization in their vicinity, but the underlying mechanism is unknown. Here, we show that cortical microtubule stabilization sites containing CLASPs, KIF21A, LL5? and liprins are recruited to focal adhesions by the adaptor protein KANK1, which directly interacts with the major adhesion component, talin. Structural studies showed that the conserved KN domain in KANK1 binds to the talin rod domain R7. Perturbation of this interaction, including a single point mutation in talin, which disrupts KANK1 binding but not the talin function in adhesion, abrogates the association of microtubule-stabilizing complexes with focal adhesions. We propose that the talin-KANK1 interaction links the two macromolecular assemblies that control cortical attachment of actin fibers and microtubules.

Published
2016

46. Opposite Electron-Transfer Dissociation and Higher-Energy Collisional Dissociation Fragmentation Characteristics of Proteolytic K/R(X)n and (X)nK/R Peptides Provide Benefits for Peptide Sequencing in Proteomics and Phosphoproteomics

Author

Tsiatsiani, Liana, primary, Giansanti, Piero, additional, Scheltema, Richard A., additional, van den Toorn, Henk, additional, Overall, Christopher M., additional, Altelaar, A.F. Maarten, additional, and Heck, Albert J.R., additional

Published
2016
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47. BRAF V600E Kinase Domain Duplication Identified in Therapy-Refractory Melanoma Patient-Derived Xenografts

Author

Kemper, Kristel, primary, Krijgsman, Oscar, additional, Kong, Xiangjun, additional, Cornelissen-Steijger, Paulien, additional, Shahrabi, Aida, additional, Weeber, Fleur, additional, van der Velden, Daphne L., additional, Bleijerveld, Onno B., additional, Kuilman, Thomas, additional, Kluin, Roel J.C., additional, Sun, Chong, additional, Voest, Emile E., additional, Ju, Young Seok, additional, Schumacher, Ton N.M., additional, Altelaar, A.F. Maarten, additional, McDermott, Ultan, additional, Adams, David J., additional, Blank, Christian U., additional, Haanen, John B., additional, and Peeper, Daniel S., additional

Published
2016
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49. Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics

Author

Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Götzke, Hansjörg, Muheim, Claudio, Altelaar, A.F. Maarten, Heck, Albert J.R., Maddalo, Gianluca, Daley, Daniel O., Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Götzke, Hansjörg, Muheim, Claudio, Altelaar, A.F. Maarten, Heck, Albert J.R., Maddalo, Gianluca, and Daley, Daniel O.

Published
2015

50. A novel Fanconi anemia subtype associated with a dominant-negative mutation in RAD51

Author

Luxembourg Centre for Systems Biomedicine (LCSB): Bioinformatics Core (R. Schneider Group) [research center], Luxembourg Centre for Systems Biomedicine (LCSB): Experimental Neurobiology (Balling Group) [research center], University of Luxembourg: High Performance Computing - ULHPC [research center], Ameziane, Najim, May, Patrick, Van de Vrugt, Henri J., Van Rossum-Fikkert, Sari E., Ristic, Dejan, Williams, Gareth J., Balk, Jesper, Rockx, Davy, Li, Hong, Rooimans, Martin A., Oostra, Anneke B., Velleuer, Eunike, Dietrich, Ralf, Bleijerveld, Onno B., Altelaar, A.F. Maarten, Meijers-Heijboer, Hanne, Joenje, Hans, Glusman, Gustavo, Roach, Jared C., Hood, Leroy, Galas, David J., Balling, Rudi, den Dunnen, Johan, De Winter, Johan P., Kanaar, Roland, Gelinas, Richard, Dorsman, Josephine C., Luxembourg Centre for Systems Biomedicine (LCSB): Bioinformatics Core (R. Schneider Group) [research center], Luxembourg Centre for Systems Biomedicine (LCSB): Experimental Neurobiology (Balling Group) [research center], University of Luxembourg: High Performance Computing - ULHPC [research center], Ameziane, Najim, May, Patrick, Van de Vrugt, Henri J., Van Rossum-Fikkert, Sari E., Ristic, Dejan, Williams, Gareth J., Balk, Jesper, Rockx, Davy, Li, Hong, Rooimans, Martin A., Oostra, Anneke B., Velleuer, Eunike, Dietrich, Ralf, Bleijerveld, Onno B., Altelaar, A.F. Maarten, Meijers-Heijboer, Hanne, Joenje, Hans, Glusman, Gustavo, Roach, Jared C., Hood, Leroy, Galas, David J., Balling, Rudi, den Dunnen, Johan, De Winter, Johan P., Kanaar, Roland, Gelinas, Richard, and Dorsman, Josephine C.

Abstract

Fanconi anemia (FA) is a hereditary disease featuring hypersensitivity to DNA cross-linker-induced chromosomal instability in association with developmental abnormalities, bone marrow failure and a strong predisposition to cancer. 17 FA disease genes have been reported, all of which act in a recessive mode of inheritance. Here we report on a de novo g.41022153G>A; p.Ala293Thr (NM_002875) missense mutation in one allele of the homologous recombination DNA repair gene RAD51 in an FA-like patient. This heterozygous mutation causes a novel FA subtype, “FA-R”, which appears to be the first subtype of FA caused by a dominant-negative mutation. The patient, who features microcephaly and mental retardation, has reached adulthood without the typical bone marrow failure and pediatric cancers. Together with the recent reports on RAD51-associated congenital mirror movement disorders our results point to an important role for RAD51-mediated homologous recombination in neurodevelopment, in addition to DNA repair and cancer susceptibility.

Published
2015

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