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1. In planta expression of human polyQ-expanded huntingtin fragment reveals mechanisms to prevent disease-related protein aggregation

Author

Llamas, Ernesto, Koyuncu, Seda, Lee, Hyun Ju, Wehrmann, Markus, Gutierrez-Garcia, Ricardo, Dunken, Nick, Charura, Nyasha, Torres-Montilla, Salvador, Schlimgen, Elena, Mandel, Amrei M., Theile, Erik Boelen, Grossbach, Jan, Wagle, Prerana, Lackmann, Jan-Wilm, Schermer, Bernhard, Benzing, Thomas, Beyer, Andreas, Pulido, Pablo, Rodriguez-Concepcion, Manuel, Zuccaro, Alga, and Vilchez, David

Published
2023
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7. Experiences of insecurity among non-standard workers across different welfare states: A qualitative cross-country study

Author

Bosmans, Kim, Vignola, Emilia F., Álvarez-López, Valentina, Julià, Mireia, Ahonen, Emily Q., Bolíbar, Mireia, Gutiérrez-Zamora, Mariana, Ivarsson, Lars, Kvart, Signild, Muntaner, Carles, O'Campo, Patricia, Ruiz, Marisol E., Vänerhagen, Kristian, Cuervo, Isabel, Davis, Letitia, Diaz, Ignacio, Escrig-Piñol, Astrid, Gunn, Virginia, Lewchuk, Wayne, Östergren, Per-Olof, Padrosa, Eva, Vílchez, David, Vives, Alejandra, Vos, Mattias, Zaupa, Alessandro, Bodin, Theo, and Baron, Sherry L.

Published
2023
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11. Rewiring of the ubiquitinated proteome determines ageing in C. elegans

Author

Koyuncu, Seda, Loureiro, Rute, Lee, Hyun Ju, Wagle, Prerana, Krueger, Marcus, and Vilchez, David

Subjects
Biological research, Biology, Experimental, Caenorhabditis elegans -- Physiological aspects -- Genetic aspects, Aging -- Research, Ubiquitin -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Ageing is driven by a loss of cellular integrity.sup.1. Given the major role of ubiquitin modifications in cell function.sup.2, here we assess the link between ubiquitination and ageing by quantifying whole-proteome ubiquitin signatures in Caenorhabditis elegans. We find a remodelling of the ubiquitinated proteome during ageing, which is ameliorated by longevity paradigms such as dietary restriction and reduced insulin signalling. Notably, ageing causes a global loss of ubiquitination that is triggered by increased deubiquitinase activity. Because ubiquitination can tag proteins for recognition by the proteasome.sup.3, a fundamental question is whether deficits in targeted degradation influence longevity. By integrating data from worms with a defective proteasome, we identify proteasomal targets that accumulate with age owing to decreased ubiquitination and subsequent degradation. Lowering the levels of age-dysregulated proteasome targets prolongs longevity, whereas preventing their degradation shortens lifespan. Among the proteasomal targets, we find the IFB-2 intermediate filament.sup.4 and the EPS-8 modulator of RAC signalling.sup.5. While increased levels of IFB-2 promote the loss of intestinal integrity and bacterial colonization, upregulation of EPS-8 hyperactivates RAC in muscle and neurons, and leads to alterations in the actin cytoskeleton and protein kinase JNK. In summary, age-related changes in targeted degradation of structural and regulatory proteins across tissues determine longevity. Global loss of targeted protein degradation with age results in harmful accumulation of specific proteins in worms., Author(s): Seda Koyuncu [sup.1] , Rute Loureiro [sup.1] , Hyun Ju Lee [sup.1] , Prerana Wagle [sup.1] , Marcus Krueger [sup.1] [sup.2] , David Vilchez [sup.1] [sup.2] [sup.3] Author Affiliations: [...]

Published
2021
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12. Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy

Author

Vilchez, David, Ros, Susana, Cifuentes, Daniel, Pujadas, Lluís, Vallès, Jordi, García-Fojeda García-Valdecasas, María Belén, Criado-García, Olga, Fernández-Sánchez, Elena, Medraño-Fernández, Iria, Domínguez, Jorge, García-Rocha, Mar, Soriano, Eduardo, Rodríguez de Córdoba, Santiago, Guinovart, Joan J., Vilchez, David, Ros, Susana, Cifuentes, Daniel, Pujadas, Lluís, Vallès, Jordi, García-Fojeda García-Valdecasas, María Belén, Criado-García, Olga, Fernández-Sánchez, Elena, Medraño-Fernández, Iria, Domínguez, Jorge, García-Rocha, Mar, Soriano, Eduardo, Rodríguez de Córdoba, Santiago, and Guinovart, Joan J.

Abstract

Glycogen synthesis is normally absent in neurons. However, inclusion bodies resembling abnormal glycogen accumulate in several neurological diseases, particularly in progressive myoclonus epilepsy or Lafora disease. We show here that mouse neurons have the enzymatic machinery for synthesizing glycogen, but that it is suppressed by retention of muscle glycogen synthase (MGS) in the phosphorylated, inactive state. This suppression was further ensured by a complex of laforin and malin, which are the two proteins whose mutations cause Lafora disease. The laforin-malin complex caused proteasome-dependent degradation both of the adaptor protein targeting to glycogen, PTG, which brings protein phosphatase 1 to MGS for activation, and of MGS itself. Enforced expression of PTG led to glycogen deposition in neurons and caused apoptosis. Therefore, the malin-laforin complex ensures a blockade of neuronal glycogen synthesis even under intense glycogenic conditions. Here we explain the formation of polyglucosan inclusions in Lafora disease by demonstrating a crucial role for laforin and malin in glycogen synthesis., Ministerio de Educación y Ciencia, Instituto de Salud Carlos III, Fundació La Caixa, Fundació La Marató de TV3, Fundación Marcelino Botín, Depto. de Bioquímica y Biología Molecular, Fac. de Ciencias Químicas, TRUE, pub

Published
2024

15. Arabidopsis metacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence

Author

Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Ministerio de Economía y Competitividad (España), European Commission, Generalitat de Catalunya, Ministerio de Universidades (España), German Research Foundation, Else Kröner-Fresenius Foundation, European Cooperation in Science and Technology, CSIC - Unidad de Recursos de Información Científica para la Investigación (URICI), Ruiz-Solaní, Nerea [0000-0002-0813-0956], Salguero-Linares, José Manuel [0000-0003-0559-7793], Armengot, Laia [0000-0002-3790-9838], Santos, Jaime [0000-0001-9045-7765], Pallarès, Irantzu [0000-0002-8205-2060], Midden, Katarina P. [0000-0002-4962-5410], Phukkan, Ujjal J. [0000-0001-9788-4938], Koyuncu, Seda [0000-0001-7937-3974], Borràs-Bisa, Júlia [0009-0009-0096-9990], Li, Liang [0009-0003-2816-1885], Popa, Crina [0000-0002-4294-9949], Eisele, Frederik [0000-0001-9995-5816], Eisele-Bürger, Anna Maria [0000-0002-4009-094X], Hill, S. M. [0000-0001-7969-097X], Gutierrez-Beltran, Emilio [0000-0001-7978-3164], Nyström, Thomas [0000-0001-5489-2903], Valls, Marc [0000-0003-2312-0091], Llamas, Ernesto [0000-0001-9262-2402], Vilchez, David [0000-0002-0801-0743], Klemenčič, Marina [0000-0002-3079-4492], Ventura, Salvador [0000-0002-9652-6351], Coll, Núria S. [0000-0002-8889-0399], Ruiz-Solaní, Nerea, Salguero-Linares, José Manuel, Armengot, Laia, Santos, Jaime, Pallarès, Irantzu, Midden, Katarina P. van, Phukkan, Ujjal J., Koyuncu, Seda, Borràs-Bisa, Júlia, Li, Liang, Popa, Crina, Eisele, Frederik, Eisele-Bürger, Anna Maria, Hill, S. M., Gutierrez-Beltran, Emilio, Nyström, Thomas, Valls, Marc, Llamas, Ernesto, Vilchez, David, Klemenčič, Marina, Ventura, Salvador, Coll, Núria S., Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Ministerio de Economía y Competitividad (España), European Commission, Generalitat de Catalunya, Ministerio de Universidades (España), German Research Foundation, Else Kröner-Fresenius Foundation, European Cooperation in Science and Technology, CSIC - Unidad de Recursos de Información Científica para la Investigación (URICI), Ruiz-Solaní, Nerea [0000-0002-0813-0956], Salguero-Linares, José Manuel [0000-0003-0559-7793], Armengot, Laia [0000-0002-3790-9838], Santos, Jaime [0000-0001-9045-7765], Pallarès, Irantzu [0000-0002-8205-2060], Midden, Katarina P. [0000-0002-4962-5410], Phukkan, Ujjal J. [0000-0001-9788-4938], Koyuncu, Seda [0000-0001-7937-3974], Borràs-Bisa, Júlia [0009-0009-0096-9990], Li, Liang [0009-0003-2816-1885], Popa, Crina [0000-0002-4294-9949], Eisele, Frederik [0000-0001-9995-5816], Eisele-Bürger, Anna Maria [0000-0002-4009-094X], Hill, S. M. [0000-0001-7969-097X], Gutierrez-Beltran, Emilio [0000-0001-7978-3164], Nyström, Thomas [0000-0001-5489-2903], Valls, Marc [0000-0003-2312-0091], Llamas, Ernesto [0000-0001-9262-2402], Vilchez, David [0000-0002-0801-0743], Klemenčič, Marina [0000-0002-3079-4492], Ventura, Salvador [0000-0002-9652-6351], Coll, Núria S. [0000-0002-8889-0399], Ruiz-Solaní, Nerea, Salguero-Linares, José Manuel, Armengot, Laia, Santos, Jaime, Pallarès, Irantzu, Midden, Katarina P. van, Phukkan, Ujjal J., Koyuncu, Seda, Borràs-Bisa, Júlia, Li, Liang, Popa, Crina, Eisele, Frederik, Eisele-Bürger, Anna Maria, Hill, S. M., Gutierrez-Beltran, Emilio, Nyström, Thomas, Valls, Marc, Llamas, Ernesto, Vilchez, David, Klemenčič, Marina, Ventura, Salvador, and Coll, Núria S.

Abstract

Stress granules (SGs) are highly conserved cytoplasmic condensates that assemble in response to stress and contribute to maintaining protein homeostasis. These membraneless organelles are dynamic, disassembling once the stress is no longer present. Persistence of SGs due to mutations or chronic stress has been often related to age-dependent protein-misfolding diseases in animals. Here, we find that the metacaspase MC1 is dynamically recruited into SGs upon proteotoxic stress in Arabidopsis (Arabidopsis thaliana). Two predicted disordered regions, the prodomain and the 360 loop, mediate MC1 recruitment to and release from SGs. Importantly, we show that MC1 has the capacity to clear toxic protein aggregates in vivo and in vitro, acting as a disaggregase. Finally, we demonstrate that overexpressing MC1 delays senescence and this phenotype is dependent on the presence of the 360 loop and an intact catalytic domain. Together, our data indicate that MC1 regulates senescence through its recruitment into SGs and this function could potentially be linked to its remarkable protein aggregate-clearing activity.

Published
2023

16. SPTF-3/SP1 orchestrates mitochondrial biogenesis upon ribosomal stress and acute starvation

Author

Hermeling, Johannes, primary, Pavlenko, Victor, additional, Herholz, Marija, additional, Baumaann, Linda, additional, Zecic, Aleksandra, additional, Kukat, Alexandra, additional, Popovic, Milica, additional, Szczepanowska, Kaarolina, additional, Cepeda Cores, Estela, additional, Vilchez, David, additional, Kurian, Leo, additional, and Trifunovic, Aleksandra, additional

Published
2023
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22. Arabidopsismetacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence

Author

Ruiz-Solaní, Nerea, primary, Salguero-Linares, Jose, additional, Armengot, Laia, additional, Santos, Jaime, additional, Pallarès, Irantzu, additional, van Midden, Katarina P, additional, Phukkan, Ujjal J, additional, Koyuncu, Seda, additional, Borràs-Bisa, Júlia, additional, Li, Liang, additional, Popa, Crina, additional, Eisele, Frederik, additional, Eisele-Bürger, Anna Maria, additional, Hill, Sandra Malgrem, additional, Gutiérrez-Beltrán, Emilio, additional, Nyström, Thomas, additional, Valls, Marc, additional, Llamas, Ernesto, additional, Vilchez, David, additional, Klemenčič, Marina, additional, Ventura, Salvador, additional, and Coll, Nuria S, additional

Published
2023
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28. Usage of iron foliar spray in enhancing the growth and yield of the flax plant (Linum usitatissimum L)

Author

Gondal, Aqarab Husnain, primary, Areche, Franklin Ore, additional, Sumarriva-Bustinza, Liliana Asunción, additional, Chávez-Sumarriva, Nadia Lys, additional, Zela-Payi, Nelly Olga, additional, More López, Jesús Manuel, additional, Saldarriaga, José Yovera, additional, García-Díaz, Bertila Liduvina, additional, Porras-Roque, María Soledad, additional, Ayuque-Rojas, Jose Carlos, additional, Aguilar, Salomón Vivanco, additional, Vilchez, David Ruiz, additional, Yaulilahua-Huacho, Russbelt, additional, Malpartida Yapias, Rafael Julian, additional, and Jabbar, Abdul, additional

Published
2023
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31. Supplementary Data of the article Arabidopsis metacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence

Author

Ruiz-Solaní, Nerea, Salguero-Linares, José Manuel, Armengot, Laia, Santos, Jaime, Pallarès, Irantzu, Midden, Katarina P. van, Phukkan, Ujjal J., Koyuncu, Seda, Borràs-Bisa, Júlia, Li, Liang, Popa, Crina, Eisele, Frederik, Eisele-Bürger, Anna Maria, Hill, S. M., Gutierrez-Beltran, Emilio, Nyström, Thomas, Valls, Marc, Llamas, Ernesto, Vilchez, David, Klemenčič, Marina, Ventura, Salvador, Coll, Núria S., Ruiz-Solaní, Nerea, Salguero-Linares, José Manuel, Armengot, Laia, Santos, Jaime, Pallarès, Irantzu, Midden, Katarina P. van, Phukkan, Ujjal J., Koyuncu, Seda, Borràs-Bisa, Júlia, Li, Liang, Popa, Crina, Eisele, Frederik, Eisele-Bürger, Anna Maria, Hill, S. M., Gutierrez-Beltran, Emilio, Nyström, Thomas, Valls, Marc, Llamas, Ernesto, Vilchez, David, Klemenčič, Marina, Ventura, Salvador, and Coll, Núria S.

Published
2023

32. Arabidopsis metacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence.

Author

Ruiz-Solaní, Nerea, Salguero-Linares, Jose, Armengot, Laia, Santos, Jaime, Pallarès, Irantzu, van Midden, Katarina P, Phukkan, Ujjal J, Koyuncu, Seda, Borràs-Bisa, Júlia, Li, Liang, Popa, Crina, Eisele, Frederik, Eisele-Bürger, Anna Maria, Hill, Sandra Malgrem, Gutiérrez-Beltrán, Emilio, Nyström, Thomas, Valls, Marc, Llamas, Ernesto, Vilchez, David, and Klemenčič, Marina

Published
2023
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40. A dimer-monomer switch controls CHIP-dependent substrate ubiquitylation and processing

Author

Balaji, Vishnu, Mueller, Leonie, Lorenz, Robin, Kevei, Eva, Zhang, William H., Santiago, Ulises, Gebauer, Jan, Llamas, Ernesto, Vilchez, David, Camacho, Carlos J., Pokrzywa, Wojciech, Hoppe, Thorsten, Balaji, Vishnu, Mueller, Leonie, Lorenz, Robin, Kevei, Eva, Zhang, William H., Santiago, Ulises, Gebauer, Jan, Llamas, Ernesto, Vilchez, David, Camacho, Carlos J., Pokrzywa, Wojciech, and Hoppe, Thorsten

Abstract

The high substrate selectivity of the ubiquitin/proteasome system is mediated by a large group of E3 ubiquitin ligases. The ubiquitin ligase CHIP regulates the degradation of chaperone-controlled and chaperone -inde-pendent proteins. To understand how CHIP mediates substrate selection and processing, we performed a structure-function analysis of CHIP and addressed its physiological role in Caenorhabditis elegans and hu-man cells. The conserved function of CHIP in chaperone-assisted degradation requires dimer formation to mediate proteotoxic stress resistance and to prevent protein aggregation. The CHIP monomer, however, promotes the turnover of the membrane-bound insulin receptor and longevity. The dimer-monomer transition is regulated by CHIP autoubiquitylation and chaperone binding, which provides a feedback loop that controls CHIP activity in response to cellular stress. Because CHIP also binds other E3 ligases, such as Parkin, the molecular switch mechanism described here could be a general concept for the regulation of substrate selec-tivity and ubiquitylation by combining different E3s.

Published
2022

43. Chloroplast protein import determines plant proteostasis and retrograde signaling

Author

Llamas, Ernesto, primary, Koyuncu, Seda, additional, Lee, Hyun Ju, additional, Gutierrez-Garcia, Ricardo, additional, Dunken, Nick, additional, Charura, Nyasha, additional, Torres-Montilla, Salvador, additional, Schlimgen, Elena, additional, Pulido, Pablo, additional, Rodriguez-Concepcion, Manuel, additional, Zuccaro, Alga, additional, and Vilchez, David, additional

Published
2022
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46. Análise do conhecimento das puérperas em situação de emergência com os bebês

Author

Luiza Vilchez David, Maria Virginia Godoy da Silva, Juliana Lana Querino de Oliveira, Abilene do Nascimento Gouvêa, Vladimir Chaves Fernandes, Elson Santos de Oliveira, and Marcos José Vilchez David

Subjects
Nursing, Health professionals, media_common.quotation_subject, General Earth and Planetary Sciences, Assertiveness, Psychology, University hospital, Know-how, Emergency situations, General Environmental Science, media_common, First aid
Abstract

Objetivo: Analisar o conhecimento das puérperas em situações de emergência domésticas que envolvam os lactentes. Metodologia: Trata-se de um estudo exploratório com abordagem quantitativa realizado no mês de maio de 2021 em um hospital universitário localizada na cidade do Rio de Janeiro. A coleta de dados foi por meio de questionários anônimos, com perguntas estruturadas, de modo fechado, auto preenchidos pelas puérperas. Resultados: A partir desta pesquisa, contatou-se que 83% das puérperas entrevistadas não receberam durante as consultas de pré-natal, algum ensinamento sobre primeiros socorros aos lactentes pelo profissional da saúde que a assistia. Além deste ponto destacado, vale ressaltar que 100% das entrevistadas gostariam de receber informações dos profissionais da saúde de como prestar socorro aos bebês. Conclusão: Se as grávidas e puérperas tivessem, durante as consultas de pré-natal e pós-natal, algum ensinamento ou orientação pelo profissional da saúde sobre como agir em situações de emergência com o bebê, os problemas seriam mais fáceis de diagnosticar, pois as mães saberiam identificar o que o filho apresenta e saberiam prestar um atendimento assertivo para aumentar a sobrevida da vítima. O profissional da saúde que assistiria esta puérpera, deveria dar um enfoque maior em como prestar atendimento em vítimas com obstrução de vias aéreas, queimadura por temperaturas elevadas e crise convulsiva, pois a partir do estudo desta pesquisa, pode-se observar que estas foram as questões que as puérperas possuem maior dúvida.

Published
2021

47. The intrinsic chaperone network of Arabidopsis stem cells confers protection against proteotoxic stress

Author

Llamas, Ernesto, primary, Torres‐Montilla, Salvador, additional, Lee, Hyun Ju, additional, Barja, María Victoria, additional, Schlimgen, Elena, additional, Dunken, Nick, additional, Wagle, Prerana, additional, Werr, Wolfgang, additional, Zuccaro, Alga, additional, Rodríguez‐Concepción, Manuel, additional, and Vilchez, David, additional

Published
2021
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49. The intrinsic chaperone network of Arabidopsis stem cells confers protection against proteotoxic stress

Author

Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes, European Commission, Deutsche Forschungsgemeinschaft, Llamas, Ernesto, Torres-Montilla, Salvador, Lee, Hyun Ju, Barja, María Victoria, Schlimgen, Elena, Dunken, Nick, Wagle, Prerana, Werr, Wolfgang, Zuccaro, Alga, RODRIGUEZ CONCEPCIÓN, M., Vilchez, David, Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes, European Commission, Deutsche Forschungsgemeinschaft, Llamas, Ernesto, Torres-Montilla, Salvador, Lee, Hyun Ju, Barja, María Victoria, Schlimgen, Elena, Dunken, Nick, Wagle, Prerana, Werr, Wolfgang, Zuccaro, Alga, RODRIGUEZ CONCEPCIÓN, M., and Vilchez, David

Abstract

[EN] The biological purpose of plant stem cells is to maintain themselves while providing new pools of differentiated cells that form organs and rejuvenate or replace damaged tissues. Protein homeostasis or proteostasis is required for cell function and viability. However, the link between proteostasis and plant stem cell identity remains unknown. In contrast to their differentiated counterparts, we find that root stem cells can prevent the accumulation of aggregated proteins even under proteotoxic stress conditions such as heat stress or proteasome inhibition. Notably, root stem cells exhibit enhanced expression of distinct chaperones that maintain proteome integrity. Particularly, intrinsic high levels of the T-complex protein-1 ring complex/chaperonin containing TCP1 (TRiC/CCT) complex determine stem cell maintenance and their remarkable ability to suppress protein aggregation. Overexpression of CCT8, a key activator of TRiC/CCT assembly, is sufficient to ameliorate protein aggregation in differentiated cells and confer resistance to proteotoxic stress in plants. Taken together, our results indicate that enhanced proteostasis mechanisms in stem cells could be an important requirement for plants to persist under extreme environmental conditions and reach extreme long ages. Thus, proteostasis of stem cells can provide insights to design and breed plants tolerant to environmental challenges caused by the climate change.

Published
2021

50. The intrinsic chaperone network of Arabidopsis stem cells confers protection against proteotoxic stress

Author

Llamas, Ernesto, Torres-Montilla, Salvador, Lee, Hyun Ju, Barja, Maria Victoria, Schlimgen, Elena, Dunken, Nick, Wagle, Prerana, Werr, Wolfgang, Zuccaro, Alga, Rodriguez-Concepcion, Manuel, Vilchez, David, Llamas, Ernesto, Torres-Montilla, Salvador, Lee, Hyun Ju, Barja, Maria Victoria, Schlimgen, Elena, Dunken, Nick, Wagle, Prerana, Werr, Wolfgang, Zuccaro, Alga, Rodriguez-Concepcion, Manuel, and Vilchez, David

Abstract

The biological purpose of plant stem cells is to maintain themselves while providing new pools of differentiated cells that form organs and rejuvenate or replace damaged tissues. Protein homeostasis or proteostasis is required for cell function and viability. However, the link between proteostasis and plant stem cell identity remains unknown. In contrast to their differentiated counterparts, we find that root stem cells can prevent the accumulation of aggregated proteins even under proteotoxic stress conditions such as heat stress or proteasome inhibition. Notably, root stem cells exhibit enhanced expression of distinct chaperones that maintain proteome integrity. Particularly, intrinsic high levels of the T-complex protein-1 ring complex/chaperonin containing TCP1 (TRiC/CCT) complex determine stem cell maintenance and their remarkable ability to suppress protein aggregation. Overexpression of CCT8, a key activator of TRiC/CCT assembly, is sufficient to ameliorate protein aggregation in differentiated cells and confer resistance to proteotoxic stress in plants. Taken together, our results indicate that enhanced proteostasis mechanisms in stem cells could be an important requirement for plants to persist under extreme environmental conditions and reach extreme long ages. Thus, proteostasis of stem cells can provide insights to design and breed plants tolerant to environmental challenges caused by the climate change.

Published
2021

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