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Originally published in Science Express on 25 October 2001
Science 23 November 2001:
Vol. 294. no. 5547, pp. 1704 - 1708
DOI: 10.1126/science.1065874
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Reports

Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy

Sue C. Bodine,1 Esther Latres,1 Susanne Baumhueter,2 Venus K.-M. Lai,1 Lorna Nunez,1 Brian A. Clarke,1 William T. Poueymirou,1 Frank J. Panaro,1 Erqian Na,1 Kumar Dharmarajan,1 Zhen-Qiang Pan,3 David M. Valenzuela,1 Thomas M. DeChiara,1 Trevor N. Stitt,1 George D. Yancopoulos,1 David J. Glass1*

Skeletal muscle adapts to decreases in activity and load by undergoing atrophy. To identify candidate molecular mediators of muscle atrophy, we performed transcript profiling. Although many genes were up-regulated in a single rat model of atrophy, only a small subset was universal in all atrophy models. Two of these genes encode ubiquitin ligases: Muscle RING Finger 1 (MuRF1), and a gene we designate Muscle Atrophy F-box (MAFbx), the latter being a member of the SCF family of E3 ubiquitin ligases. Overexpression of MAFbx in myotubes produced atrophy, whereas mice deficient in either MAFbx or MuRF1 were found to be resistant to atrophy. These proteins are potential drug targets for the treatment of muscle atrophy.

1 Regeneron Pharmaceuticals, 777 Old Saw Mill River Road, Tarrytown, NY, 10591-6707, USA.
2 Applied Biosystems, 850 Lincoln Center Drive, Foster City, CA 94404, USA.
3 Derald H. Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, NY, 10029-6574, USA.
*   To whom correspondence should be addressed. E-mail: david.glass{at}regeneron.com

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Myofibrillar protein turnover: The proteasome and the calpains.
D. E. Goll, G. Neti, S. W. Mares, and V. F. Thompson (2008)
J Anim Sci 86, E19-E35
   Abstract »    Full Text »    PDF »
Cardiac Plasticity.
J. A. Hill and E. N. Olson (2008)
N. Engl. J. Med. 358, 1370-1380
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Temporal changes in the involvement of pyruvate dehydrogenase complex in muscle lactate accumulation during lipopolysaccharide infusion in rats.
N. Alamdari, D. Constantin-Teodosiu, A. J. Murton, S. M. Gardiner, T. Bennett, R. Layfield, and P. L. Greenhaff (2008)
J. Physiol. 586, 1767-1775
   Abstract »    Full Text »    PDF »
Glucocorticoids differentially regulate degradation of MyoD and Id1 by N-terminal ubiquitination to promote muscle protein catabolism.
L. Sun, J. S. Trausch-Azar, L. J. Muglia, and A. L. Schwartz (2008)
PNAS 105, 3339-3344
   Abstract »    Full Text »    PDF »
Feeding Status Regulates the Polyubiquitination Step of the Ubiquitin-Proteasome-Dependent Proteolysis in Rainbow Trout (Oncorhynchus mykiss) Muscle.
I. Seiliez, S. Panserat, S. Skiba-Cassy, A. Fricot, C. Vachot, S. Kaushik, and S. Tesseraud (2008)
J. Nutr. 138, 487-491
   Abstract »    Full Text »    PDF »
Repeated resistance exercise training induces different changes in mRNA expression of MAFbx and MuRF-1 in human skeletal muscle.
H. Mascher, J. Tannerstedt, T. Brink-Elfegoun, B. Ekblom, T. Gustafsson, and E. Blomstrand (2008)
Am J Physiol Endocrinol Metab 294, E43-E51
   Abstract »    Full Text »    PDF »
Proteolytic Gene Expression Differs At Rest and After Resistance Exercise Between Young and Old Women.
U. Raue, D. Slivka, B. Jemiolo, C. Hollon, and S. Trappe (2007)
J Gerontol A Biol Sci Med Sci 62, 1407-1412
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Evidence for Adipose-Muscle Cross Talk: Opposing Regulation of Muscle Proteolysis by Adiponectin and Fatty Acids.
Q. Zhou, J. Du, Z. Hu, K. Walsh, and X. H. Wang (2007)
Endocrinology 148, 5696-5705
   Abstract »    Full Text »    PDF »
IFN-{gamma} does not mimic the catabolic effects of TNF-{alpha}.
M. A. Smith, J. S. Moylan, J. D. Smith, W. Li, and M. B. Reid (2007)
Am J Physiol Cell Physiol 293, C1947-C1952
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The Histone Deacetylase HDAC4 Connects Neural Activity to Muscle Transcriptional Reprogramming.
T. J. Cohen, D. S. Waddell, T. Barrientos, Z. Lu, G. Feng, G. A. Cox, S. C. Bodine, and T.-P. Yao (2007)
J. Biol. Chem. 282, 33752-33759
   Abstract »    Full Text »    PDF »
Antioxidant administration attenuates mechanical ventilation-induced rat diaphragm muscle atrophy independent of protein kinase B (PKB Akt) signalling.
J. M. McClung, A. N. Kavazis, M. A. Whidden, K. C. DeRuisseau, D. J. Falk, D. S. Criswell, and S. K. Powers (2007)
J. Physiol. 585, 203-215
   Abstract »    Full Text »    PDF »


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