The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3
Open accessAbstract
Maintenance of skeletal and cardiac muscle structure and function requires precise control of the synthesis, assembly, and turnover of contractile proteins of the sarcomere. Abnormalities in accumulation of sarcomere proteins are responsible for a variety of myopathies. However, the mechanisms that mediate turnover of these long-lived proteins remain poorly defined. We show that muscle RING finger 1 (MuRF1) and MuRF3 act as E3 ubiquitin ligases that cooperate with the E2 ubiquitin-conjugating enzymes UbcH5a, -b, and -c to mediate the degradation of beta/slow myosin heavy chain (beta/slow MHC) and MHCIIa via the ubiquitin proteasome system (UPS) in vivo and in vitro. Accordingly, mice deficient for MuRF1 and MuRF3 develop a skeletal muscle myopathy and hypertrophic cardiomyopathy characterized by subsarcolemmal MHC accumulation, myofiber fragmentation, and diminished muscle performance. These findings identify MuRF1 and MuRF3 as key E3 ubiquitin ligases for the UPS-dependent turnover of sarcomeric proteins and reveal a potential basis for myosin storage myopathies.
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Identification of ubiquitin ligases required for skeletal muscle atrophy.
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Self-citationCancer cachexia is regulated by selective targeting of skeletal muscle gene products
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Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
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A Novel Nemaline Myopathy in the Amish Caused by a Mutation in Troponin T1
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Fiber Types in Mammalian Skeletal Muscles
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Mechanisms regulating skeletal muscle growth and atrophy
Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284
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Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
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“By contrast, MuRF1 and 3 double-knockout mice develop skeletal and cardiac muscle myopathy with myosin accumulation [ 99 ], and MuRF1 and 2 doubleknockout mice have mild skeletal muscle hypertrophy and have reduced muscle loss during aging [100].”
Background
Metadata
- Authors
- Fielitz, J., Kim, M.-S., Shelton, J. M., Latif, S., Spencer, J. A., Glass, D. J., Richardson, J. A., Bassel-Duby, R., & Olson, E. N.
- Venue
- Journal of Clinical Investigation
- Published
- 2007-09-04
- Volume
- 117
- Issue
- 9
- Pages
- 2486-2495
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W1966333337
- Cited by
- 271
- References
- 42
- FWCI
- 5.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Fielitz, J., Kim, M.-S., Shelton, J. M., Latif, S., Spencer, J. A., Glass, D. J., Richardson, J. A., Bassel-Duby, R., & Olson, E. N. (2007). Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. Journal of Clinical Investigation. https://doi.org/10.1172/jci32827
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