http://purl.uniprot.org/citations/14522875 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/14522875 | http://www.w3.org/2000/01/rdf-schema#comment | "Rho-binding kinase and the myosin phosphatase targeting subunit regulate nonmuscle contractile events in higher eukaryotes. Genetic evidence indicates that the C. elegans homologs regulate embryonic morphogenesis by controlling the actin-mediated epidermal cell shape changes that transform the spherical embryo into a long, thin worm. LET-502/Rho-binding kinase triggers elongation while MEL-11/myosin phosphatase targeting subunit inhibits this contractile event. We describe mutations in the nonmuscle myosin heavy chain gene nmy-1 that were isolated as suppressors of the mel-11 hypercontraction phenotype. However, a nmy-1 null allele displays elongation defects less severe than mutations in let-502 or in the single nonmuscle myosin light chain gene mlc-4. This results because nmy-1 is partially redundant with another nonmuscle myosin heavy chain, nmy-2, which was previously known only for its role in anterior/posterior polarity and cytokinesis in the early embryo. At the onset of elongation, NMY-1 forms filamentous-like structures similar to actin, and LET-502 is interspersed with these structures, where it may trigger contraction. MEL-11, which inhibits elongation, is initially cytoplasmic. In response to LET-502 activity, MEL-11 becomes sequestered away from the contractile apparatus, to the plasma membrane, when elongation commences. Upon completion of morphogenesis, MEL-11 again appears in the cytoplasm where it may halt actin/myosin contraction."xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.org/dc/terms/identifier | "doi:10.1242/dev.00807"xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/author | "Johnson J.L."xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/author | "Mains P.E."xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/author | "Piekny A.J."xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/author | "Cham G.D."xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/name | "Development"xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/pages | "5695-5704"xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/title | "The Caenorhabditis elegans nonmuscle myosin genes nmy-1 and nmy-2 function as redundant components of the let-502/Rho-binding kinase and mel-11/myosin phosphatase pathway during embryonic morphogenesis."xsd:string |
http://purl.uniprot.org/citations/14522875 | http://purl.uniprot.org/core/volume | "130"xsd:string |
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