Protein quality control gets muscle into shape.

Abstract:

:The synthesis, assembly and organisation of structural and motor proteins during muscle formation requires temporal and spatial control directed by specialized chaperones. For example, alphaB-crystallin, GimC and TRiC facilitate the assembly of sarcomeric proteins such as desmin and actin. Recent studies have demonstrated that the chaperone family of UCS proteins (UNC-45-CRO1-She4p) is required for the proper function of myosin motors. Mutations in the myosin-directed chaperone unc-45, a founding member of this family, lead to disorganisation of striated muscle in Caenorhabditiselegans. In addition to the involvement of client-specific chaperones, myofibrillogenesis also involves ubiquitin-dependent degradation of regulatory muscle proteins. Here, we highlight the interplay between chaperone activity and protein degradation in respect to the formation and maintenance of muscle during physiological and pathological conditions.

journal_name

Trends Cell Biol

journal_title

Trends in cell biology

authors

Kim J,Löwe T,Hoppe T

doi

10.1016/j.tcb.2008.03.007

subject

Has Abstract

pub_date

2008-06-01 00:00:00

pages

264-72

issue

6

eissn

0962-8924

issn

1879-3088

pii

S0962-8924(08)00132-3

journal_volume

18

pub_type

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