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Literature DB >> 12842031

UCS proteins: managing the myosin motor.

Abstract

Recent studies indicate that myosin molecular motors interact inside cells with proteins containing a conserved 'UCS' domain. This appears to ensure proper folding of myosin heads so that they can perform their ATP-dependent actin-based motor functions.

Entities: Chemical Gene

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Year: 2003 PMID： 12842031 DOI： 10.1016/s0960-9822(03)00447-0

Source DB: PubMed Journal: Curr Biol ISSN： 0960-9822 Impact factor: 10.834

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Cited

15 in total

1. Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.

Authors: Chi F Lee; Girish C Melkani; Qin Yu; Jennifer A Suggs; William A Kronert; Yoko Suzuki; Lori Hipolito; Maureen G Price; Henry F Epstein; Sanford I Bernstein
Journal: J Cell Sci Date: 2011-02-01 Impact factor: 5.285

2. UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.

Authors: Paul J Bujalowski; Paul Nicholls; Andres F Oberhauser
Journal: Biophys J Date: 2014-08-05 Impact factor: 4.033

Review 3. Getting folded: chaperone proteins in muscle development, maintenance and disease.

Authors: Daniel A Smith; Carmen R Carland; Yiming Guo; Sanford I Bernstein
Journal: Anat Rec (Hoboken) Date: 2014-09 Impact factor: 2.064

4. Drosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase.

Authors: Girish C Melkani; Chi F Lee; Anthony Cammarato; Sanford I Bernstein
Journal: Biochem Biophys Res Commun Date: 2010-04-18 Impact factor: 3.575

UCS proteins: managing the myosin motor.

1. Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.

2. UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.

Review 3. Getting folded: chaperone proteins in muscle development, maintenance and disease.

4. Drosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase.

5. X-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.

6. Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function.

7. Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells.

8. GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.

9. Lack of developmental redundancy between Unc45 proteins in zebrafish muscle development.

10. The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.