Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin

José M. Barral, Alex H. Hutagalung, Achim Brinker, F. Ulrich Hartl, Henry F. Epstein

    Research output: Contribution to journalArticle

    184 Scopus citations

    Abstract

    The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractile ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.

    Original languageEnglish (US)
    Pages (from-to)669-671
    Number of pages3
    JournalScience
    Volume295
    Issue number5555
    DOIs
    StatePublished - Jan 25 2002

    ASJC Scopus subject areas

    • General

    Fingerprint Dive into the research topics of 'Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin'. Together they form a unique fingerprint.

  • Cite this

    Barral, J. M., Hutagalung, A. H., Brinker, A., Hartl, F. U., & Epstein, H. F. (2002). Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science, 295(5555), 669-671. https://doi.org/10.1126/science.1066648