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  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. (2002). Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science, 295(5555), 669-671.

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Genre: Journal Article
Alternative Title : Science

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 Creators:
Barral, J. M.1, Author              
Hutagalung, A. H., Author
Brinker, A.1, Author              
Hartl, F. U.2, Author              
Epstein, H. F., Author
Affiliations:
1External Organizations, ou_persistent22              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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 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.

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Language(s): eng - English
 Dates: 2002-01-25
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 35342
ISI: 000173560900042
 Degree: -

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Title: Science
  Alternative Title : Science
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 295 (5555) Sequence Number: - Start / End Page: 669 - 671 Identifier: ISSN: 0036-8075