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XB-ART-50951
Int Rev Cell Mol Biol 2014 Jan 01;313:103-44. doi: 10.1016/B978-0-12-800177-6.00004-9.
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The UNC-45 myosin chaperone: from worms to flies to vertebrates.

Lee CF , Melkani GC , Bernstein SI .


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UNC-45 (uncoordinated mutant number 45) is a UCS (UNC-45, CRO1, She4p) domain protein that is critical for myosin stability and function. It likely aides in folding myosin during cellular differentiation and maintenance, and protects myosin from denaturation during stress. Invertebrates have a single unc-45 gene that is expressed in both muscle and nonmuscle tissues. Vertebrates possess one gene expressed in striated muscle (unc-45b) and another that is more generally expressed (unc-45a). Structurally, UNC-45 is composed of a series of α-helices connected by loops. It has an N-terminal tetratricopeptide repeat domain that binds to Hsp90 and a central domain composed of armadillo repeats. Its C-terminal UCS domain, which is also comprised of helical armadillo repeats, interacts with myosin. In this chapter, we present biochemical, structural, and genetic analyses of UNC-45 in Caenorhabditis elegans, Drosophila melanogaster, and various vertebrates. Further, we provide insights into UNC-45 functions, its potential mechanism of action, and its roles in human disease.

???displayArticle.pubmedLink??? 25376491
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Species referenced: Xenopus
Genes referenced: hsp90aa1.1
GO keywords: eyelid development in camera-type eye [+]

???displayArticle.disOnts??? cataract 43
???displayArticle.omims??? CATARACT 43; CTRCT43
References [+] :
Anderson, Loss of unc45a precipitates arteriovenous shunting in the aortic arches. 2008, Pubmed