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Ubiquitin-protein ligases in muscle wasting: multiple parallel pathways?PURPOSE OF REVIEW: Studies in a wide variety of animal models of muscle wasting have led to the concept that increased protein breakdown via the ubiquitin-proteasome pathway is responsible for the loss of muscle mass seen as muscle atrophy. The complexity of the ubiquitination apparatus has hampered our understanding of how this pathway is activated in atrophying muscles and which ubiquitin-conjugating enzymes in muscle are responsible. RECENT FINDINGS: Recent experiments have shown that two newly identified ubiquitin-protein ligases (E3s), atrogin-1/MAFbx and MURF-1, are critical in the development of muscle atrophy. Other in-vitro studies also implicated E2(14k) and E3alpha, of the N-end rule pathway, as playing an important role in the process. SUMMARY: It seems likely that multiple pathways of ubiquitin conjugation are activated in parallel in atrophying muscle, perhaps to target for degradation specific classes of muscle proteins. The emerging challenge will be to define the protein targets for, as well as inhibitors of, these E3s.
Document ID
20040087747
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Lecker, Stewart H.
(Beth Israel Deaconess Medical Center and Harvard Medical School Boston, Massachusetts 02215, United States)
Goldberg, A. L.
Date Acquired
August 21, 2013
Publication Date
May 1, 2003
Publication Information
Publication: Current opinion in clinical nutrition and metabolic care
Volume: 6
Issue: 3
ISSN: 1363-1950
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Review
Non-NASA Center
Review, Tutorial
NASA Discipline Musculoskeletal

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