Myosin II regulation during C. elegans embryonic elongation: LET-502/ROCK, MRCK-1 and PAK-1, three kinases with different roles
| Autor: | Sophie Quintin, Michel Labouesse, Christelle Gally, Frédéric Landmann, Hala Zahreddine, Frédéric Wissler |
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| Přispěvatelé: | Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Louis Pasteur - Strasbourg I, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Peney, Maité, Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Myosin Light Chains
Myosin light-chain kinase Recombinant Fusion Proteins Molecular Sequence Data Mutant Phosphatase macromolecular substances Protein Serine-Threonine Kinases Biology Microfilament 03 medical and health sciences 0302 clinical medicine Myosin Morphogenesis Animals Humans Protein Isoforms Amino Acid Sequence Transgenes Caenorhabditis elegans Caenorhabditis elegans Proteins Molecular Biology Cytoskeleton Actin 030304 developmental biology Myosin Type II rho-Associated Kinases 0303 health sciences Kinase Cell biology p21-Activated Kinases Phosphorylation RNA Interference Sequence Alignment 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Development (Cambridge, England) Development (Cambridge, England), Company of Biologists, 2009, 136 (18), pp.3109-19. ⟨10.1242/dev.039412⟩ Development (Cambridge, England), 2009, 136 (18), pp.3109-19. ⟨10.1242/dev.039412⟩ |
| ISSN: | 1477-9129 0950-1991 |
| DOI: | 10.1242/dev.039412⟩ |
| Popis: | International audience; Myosin II plays a central role in epithelial morphogenesis; however, its role has mainly been examined in processes involving a single cell type. Here we analyze the structure, spatial requirement and regulation of myosin II during C. elegans embryonic elongation, a process that involves distinct epidermal cells and muscles. We developed novel GFP probes to visualize the dynamics of actomyosin remodeling, and found that the assembly of myosin II filaments, but not actin microfilaments, depends on the myosin regulatory light chain (MLC-4) and essential light chain (MLC-5, which we identified herein). To determine how myosin II regulates embryonic elongation, we rescued mlc-4 mutants with various constructs and found that MLC-4 is essential in a subset of epidermal cells. We show that phosphorylation of two evolutionary conserved MLC-4 serine and threonine residues is important for myosin II activity and organization. Finally, in an RNAi screen for potential myosin regulatory light chain kinases, we found that the ROCK, PAK and MRCK homologs act redundantly. The combined loss of ROCK and PAK, or ROCK and MRCK, completely prevented embryonic elongation, but a constitutively active form of MLC-4 could only rescue a lack of MRCK. This result, together with systematic genetic epistasis tests with a myosin phosphatase mutation, suggests that ROCK and MRCK regulate MLC-4 and the myosin phosphatase. Moreover, we suggest that ROCK and PAK regulate at least one other target essential for elongation, in addition to MLC-4. |
| Databáze: | OpenAIRE |
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