4.5 Article

The UCS family of myosin chaperones

Journal

JOURNAL OF CELL SCIENCE
Volume 115, Issue 21, Pages 3983-3990

Publisher

COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.00107

Keywords

UCS; myosin; chaperone; UNC-45; protein folding

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The canonical UCS (UNC-45/Crol/She4p) protein, Caenorhabditis elegans UNC-45, was one of the earliest molecules to be shown genetically to be necessary for sarcomere assembly. Genetic analyses of homologues in several fungal species indicate that the conserved UCS domain functionally interacts with conventional type II and unconventional type V myosins. In C. elegans and other invertebrate species, UNC-45 and its orthologues interact with both sarcomeric and non-sarcomeric myosins whereas, in vertebrates, there are two UNC-45 isoforms: a general cell (GC) and a striated muscle (SM) isoform. Although the mechanism of action of UCS proteins is unknown, recent biochemical studies suggest that they may act as molecular chaperones that facilitate the folding and/or maturation of myosin.

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