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          Institute: MPI für Biochemie     Collection: Cellular Biochemistry (F.-U. Hartl)     Display Documents



ID: 35342.0, MPI für Biochemie / Cellular Biochemistry (F.-U. Hartl)
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
Authors:Barral, J. M.; Hutagalung, A. H.; Brinker, A.; Hartl, F. U.; Epstein, H. F.
Language:English
Date of Publication (YYYY-MM-DD):2002-01-25
Title of Journal:Science
Journal Abbrev.:Science
Volume:295
Issue / Number:5555
Start Page:669
End Page:671
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Comment of the Author/Creator:Date: 2002, JAN 25
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Cellular Biochemistry (F.-U. Hartl)
External Affiliations:Baylor Coll Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA; Baylor Coll Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA; Baylor Coll Med, Dept Neurol, Houston, TX 77030 USA
Identifiers:ISI:000173560900042 [ID No:1]
ISSN:0036-8075 [ID No:2]
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