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doi: 10.1242/10.1242/jcs.00107

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Journal of Cell Science 115, 3983-3990 (2002)
Copyright © 2002 The Company of Biologists Limited
doi: 10.1242/jcs.00107

Commentary

The UCS family of myosin chaperones

Alex H. Hutagalung1, Megan L. Landsverk1, Maureen G. Price2 and Henry F. Epstein1,2,*

1 Departments of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA
2 Department of Neurology, Baylor College of Medicine, Houston, TX 77030, USA

* Author for correspondence (e-mail: hepstein{at}bcm.tmc.edu)

The canonical UCS (UNC-45/Cro1/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.

Key words: UCS, Myosin, chaperone, UNC-45, Protein folding


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