Identification of novel MYO18A interaction partners required for myoblast adhesion and muscle integrity
| Autor: | Stefan Heller, Jian-Meng Cao, Xiao-Ning Cheng, Zhigang Xu, Shang-Qi Li, De-Li Shi |
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| Přispěvatelé: | Shandong University, Stanford School of Medicine [Stanford], Stanford Medicine, Stanford University-Stanford University, Induction et différenciation au cours du développement embryonnaire des vertébrés = Induction and diferentiation during vertebrate embryonic development (LBD-E11), Laboratoire de Biologie du Développement (LBD), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
PDZ domain Oligonucleotides Vesicular Transport Proteins Golgi Apparatus Myosins Biology Article Myoblasts 03 medical and health sciences symbols.namesake 0302 clinical medicine Protein Domains Two-Hybrid System Techniques Myosin Cell Adhesion Animals Humans Myocyte Cell adhesion [SDV.BDD]Life Sciences [q-bio]/Development Biology Zebrafish Actin Adaptor Proteins Signal Transducing Multidisciplinary Sarcolemma ras-GRF1 Gene Expression Profiling Muscles Tumor Suppressor Proteins Musculoskeletal development Extracellular matrix Golgi apparatus Actins Cell biology HEK293 Cells 030104 developmental biology Gene Expression Regulation symbols biology.protein Dystrophin Chickens 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, 2016, 6, pp.36768 ⟨10.1038/srep36768⟩ Scientific Reports, Nature Publishing Group, 2016, 6, pp.36768 ⟨10.1038/srep36768⟩ |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep36768⟩ |
| Popis: | The unconventional myosin MYO18A that contains a PDZ domain is required for muscle integrity during zebrafish development. However, the mechanism by which it functions in myofibers is not clear. The presence of a PDZ domain suggests that MYO18A may interact with other partners to perform muscle-specific functions. Here we performed double-hybrid screening and co-immunoprecipitation to identify MYO18A-interacting proteins, and have identified p190RhoGEF and Golgin45 as novel partners for the MYO18A PDZ domain. We have also identified Lurap1, which was previously shown to bind MYO18A. Functional analyses indicate that, similarly as myo18a, knockdown of lurap1, p190RhoGEF and Golgin45 by morpholino oligonucleotides disrupts dystrophin localization at the sarcolemma and produces muscle lesions. Simultaneous knockdown of myo18a with either of these genes severely disrupts myofiber integrity and dystrophin localization, suggesting that they may function similarly to maintain myofiber integrity. We further show that MYO18A and its interaction partners are required for adhesion of myoblasts to extracellular matrix, and for the formation of the Golgi apparatus and organization of F-actin bundles in myoblast cells. These findings suggest that MYO18A has the potential to form a multiprotein complex that links the Golgi apparatus to F-actin, which regulates muscle integrity and function during early development. |
| Databáze: | OpenAIRE |
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