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 Bioljournal_title
Trends in cell biologyauthors
Kim J,Löwe T,Hoppe Tdoi
10.1016/j.tcb.2008.03.007subject
Has Abstractpub_date
2008-06-01 00:00:00pages
264-72issue
6eissn
0962-8924issn
1879-3088pii
S0962-8924(08)00132-3journal_volume
18pub_type
杂志文章,评审abstract::The mitochondrial electron transport chain is the major source for the production of oxygen radicals. Mitochondria-generated reactive oxygen species (mROS) have been implicated in decreasing the life span and contributing to age-related diseases (known as the free radical theory of aging). Recently, the serine/threoni...
journal_title:Trends in cell biology
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journal_title:Trends in cell biology
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journal_title:Trends in cell biology
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journal_title:Trends in cell biology
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pub_type: 杂志文章,评审
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journal_title:Trends in cell biology
pub_type: 杂志文章,评审
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