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

被引：209

作者：

Barral, JM

Hutagalung, AH

Brinker, A

Hartl, FU

Epstein, HF ^{[1
]}

机构：

[1] Baylor Coll Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA

[2] Baylor Coll Med, Dept Neurol, Houston, TX 77030 USA

[3] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

SCIENCE | 2002年 / 295卷 / 5555期

关键词：

D O I：

10.1126/science.1066648

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：669 / 671

页数：3

共 31 条

[1] Caenorhabditis elegans UNC-45 is a component of muscle thick filaments and colocalizes with myosin heavy chain B, but not myosin heavy chain A [J].