CGC Bibliography Paper 5090

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

Barral JM, Hutagalung AH, Brinker A, Hartl FU, Epstein HF

Medline:

11809970

Citation:

Science 295: 669-671 2002

Type:

ARTICLE

Genes:

unc-45

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.