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Chaperoning myosins

UCS proteins, such as C. elegans UNC-45, are essential for a variety of actin- and myosin- dependent processes in fungi, nematodes and Drosophila and have now been shown to exist in mammals. Originally thought to have a catalytic activity necessary for the formation of myofilament arrays, these proteins seem in fact to function as client-specific chaperones that facilitate folding of myosin motors. In a Commentary on p. 3983, Henry Epstein and coworkers discuss the experiments that led to this idea. Genetic analyses revealed that UNC-45 and its fungal relatives interact with conventional and unconventional myosins through a conserved UCS domain. Subsequently, experiments using recombinant UNC-45 showed that it forms a complex with muscle myosin and the chaperones Hsp90 and Hsp70 and that UNC-45 itself has general chaperone activity. Interestingly, vertebrates possess two distinct UNC-45 isoforms — a general cell isoform and a striated muscle isoform — which could have distinct roles in cytoskeletal maintenance and striated muscle differentiation, respectively (see p. 4013).

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The UCS family of myosin chaperones

Alex H. Hutagalung, Megan L. Landsverk, Maureen G. Price, and Henry F. Epstein
JCS 2002 115: 3983-3990. [Abstract] [Full Text]  

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?