Myosin chaperones.

Abstract:

:The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function. The activities of the myosin-specific UCS (UNC-45/Cro1/She4) chaperones range from assisting acto-myosin dependent transport processes to scaffolding multi-subunit chaperone complexes, which are required to assemble myofilaments. Recent structure-function studies revealed the structural organization of TPR (tetratricopeptide repeat)-containing and TPR-less UCS chaperones. The observed structural differences seem to reflect the specialized and remarkably versatile working mechanisms of myosin-directed chaperones, as will be discussed in this review.

journal_name

Curr Opin Struct Biol

authors

Hellerschmied D,Clausen T

doi

10.1016/j.sbi.2013.11.002

subject

Has Abstract

pub_date

2014-04-01 00:00:00

pages

9-15

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(13)00196-6

journal_volume

25

pub_type

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