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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5555
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pubmed:dateCreated |
2002-1-25
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pubmed:abstractText |
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 contractile 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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pubmed:keyword |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
25
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pubmed:volume |
295
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
669-71
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11809970-Amino Acid Motifs,
pubmed-meshheading:11809970-Amino Acid Sequence,
pubmed-meshheading:11809970-Animals,
pubmed-meshheading:11809970-Binding Sites,
pubmed-meshheading:11809970-Caenorhabditis elegans,
pubmed-meshheading:11809970-Caenorhabditis elegans Proteins,
pubmed-meshheading:11809970-Cell Line,
pubmed-meshheading:11809970-Cloning, Molecular,
pubmed-meshheading:11809970-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11809970-HSP90 Heat-Shock Proteins,
pubmed-meshheading:11809970-Molecular Chaperones,
pubmed-meshheading:11809970-Molecular Sequence Data,
pubmed-meshheading:11809970-Myosins,
pubmed-meshheading:11809970-Peptide Fragments,
pubmed-meshheading:11809970-Protein Binding,
pubmed-meshheading:11809970-Protein Structure, Tertiary,
pubmed-meshheading:11809970-Recombinant Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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