MURF2B, a Novel LC3-Binding Protein, Participates with MURF2A in the Switch between Autophagy and Ubiquitin Proteasome System during Differentiation of C2C12 Muscle Cells
| Autor: | Florence Delort, Patrick Vicart, Fabien Gerbal, Giuseppe Baldacci, Sofia Rybina, Eric Karsenti, Véronique Pizon |
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| Přispěvatelé: | Unité de Biologie Fonctionnelle et Adaptative (BFA (UMR_8251 / U1133)), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), European Molecular Biology Laboratory [Heidelberg] (EMBL), Matière et Systèmes Complexes (MSC (UMR_7057)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Physics Department-UFR925, Université Pierre et Marie Curie - Paris 6 (UPMC), Institut Jacques Monod (IJM (UMR_7592)), Matière et Systèmes Complexes (MSC) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Proteasome Endopeptidase Complex
Cellular differentiation lcsh:Medicine Cellular homeostasis Muscle Proteins Ubiquitin-conjugating enzyme Deubiquitinating enzyme Cell Line 03 medical and health sciences Mice 0302 clinical medicine Ubiquitin Phagosomes Autophagy Animals lcsh:Science 030304 developmental biology 0303 health sciences Multidisciplinary biology lcsh:R Cell Differentiation [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Ubiquitin ligase Cell biology Proteasome Biochemistry biology.protein lcsh:Q RNA Interference 030217 neurology & neurosurgery Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Public Library of Science, 2013, 8 (10), pp.e76140. ⟨10.1371/journal.pone.0076140⟩ PLoS ONE, 2013, 8 (10), pp.e76140. ⟨10.1371/journal.pone.0076140⟩ PLoS ONE, Vol 8, Iss 10, p e76140 (2013) |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0076140⟩ |
| Popis: | International audience; The ubiquitin proteasome system and macroautophagy are proteolytic pathways essential in the maintenance of cellular homeostasis during differentiation and remodelling of skeletal muscle. In both pathways, proteins to be degraded are tagged with polyubiquitin. In skeletal muscles, the MURF2 proteins display E3 ubiquitin ligase structure suggesting that they may covalently attach ubiquitin polypeptides to still unknown target proteins. So far only MURF2A isoforms were studied and shown to interact with p62/SQSTM1, a protein implicated in macroautophagic and ubiquitin proteasome system degradations. Here, we analyzed the MURF2B and MURF2A proteins and show that the ratio of the isoforms changes during differentiation of muscle C2C12 cells and that the shift of the isoforms expression follows the sequential activation of autophagic or proteasomal degradation. We also show that MURF2B has a functional domain needed for its interaction with LC3, a protein needed for autophagic vesicles formation. Using specific MURF2 RNAi cells we observed that MURF2A and MURF2B are both needed for the formation of autophagosomes and that in the absence of MURF2B, the cells expressing MURF2A display an activated ubiquitin proteasome system implicated in the degradation of p62/SQSTM1 by UPS. Altogether, our results indicate that MURF2A and MURF2B proteins could participate in the molecular switch between the two ubiquitin degradative pathways. |
| Databáze: | OpenAIRE |
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