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

Barral, J. M.; Hutagalung, A. H.; Brinker, A.; Hartl, F. U.; Epstein, H. F.

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

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Hartl, F. U.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6FE2-C

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 contractite 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.