The Role of the UNC-82 Protein Kinase in Organizing Myosin Filaments in Striated Muscle of Caenorhabditis elegans .

Autor:	Schiller NR; Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410., Duchesneau CD; Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410., Lane LS; Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410., Reedy AR; Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410., Manzon ER; Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410., Hoppe PE; Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410 pamela.hoppe@wmich.edu.
Jazyk:	angličtina
Zdroj:	Genetics [Genetics] 2017 Mar; Vol. 205 (3), pp. 1195-1213. Date of Electronic Publication: 2016 Dec 30.
DOI:	10.1534/genetics.116.193029
Abstrakt:	We study the mechanisms that guide the formation and maintenance of the highly ordered actin-myosin cytoskeleton in striated muscle. The UNC-82 kinase of Caenorhabditis elegans is orthologous to mammalian kinases ARK5/NUAK1 and SNARK/NUAK2. UNC-82 localizes to the M-line, and is required for proper organization of thick filaments, but its substrate and mechanism of action are unknown. Antibody staining of three mutants with missense mutations in the UNC-82 catalytic domain revealed muscle structure that is less disorganized than in the null unc-82(0) , but contained distinctive ectopic accumulations not found in unc-82(0) These accumulations contain paramyosin and myosin B, but lack myosin A and myosin A-associated proteins, as well as proteins of the integrin-associated complex. Fluorescently tagged missense mutant protein UNC-82 E424K localized normally in wild type; however, in unc-82(0) , the tagged protein was found in the ectopic accumulations, which we also show to label with recently synthesized paramyosin. Recruitment of wild-type UNC-82::GFP to aggregates of differing protein composition in five muscle-affecting mutants revealed that colocalization of UNC-82 and paramyosin does not require UNC-96, UNC-98/ZnF, UNC-89/obscurin, CSN-5, myosin A, or myosin B individually. Dosage effects in paramyosin mutants suggest that UNC-82 acts as part of a complex, in which its stoichiometric relationship with paramyosin is critical. UNC-82 dosage affects muscle organization in the absence of paramyosin, perhaps through myosin B. We present evidence that the interaction of UNC-98/ZnF with myosin A is independent of UNC-82, and that UNC-82 acts upstream of UNC-98/ZnF in a pathway that organizes paramyosin during thick filament assembly. (Copyright © 2017 by the Genetics Society of America.)
Databáze:	MEDLINE
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