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Muscle RING-finger ...
Muscle RING-finger protein-1 (MuRF1) functions and cellular localization are regulated by SUMO1 post-translational modification
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- Heras, Gabriel (författare)
- Karolinska Institutet
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- Namuduri, Arvind Venkat (författare)
- Karolinska Institutet
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- Traini, Leonardo (författare)
- Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden
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- Shevchenko, Ganna (författare)
- Uppsala universitet,Analytisk kemi,Mass spectrometry-based proteomics
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- Falk, Alexander, Research engineer, 1986- (författare)
- Uppsala universitet,Analytisk kemi,Mass spectrometry-based proteomics
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- Bergström Lind, Sara, 1977- (författare)
- Uppsala universitet,Analytisk kemi,Mass spectrometry-based proteomics
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- Mi, Jia (författare)
- Uppsala universitet,Analytisk kemi,Precision Medicine and Pharmacy Research Center, Binzhou Medical University, Yantai, China,Mass spectrometry-based proteomics
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- Tian, Geng (författare)
- Precision Medicine and Pharmacy Research Center, Binzhou Medical University, Yantai, China
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- Gastaldello, Stefano (författare)
- Karolinska Institutet
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(creator_code:org_t)
- 2018-06-04
- 2019
- Engelska.
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Ingår i: Journal of Molecular Cell Biology. - : Oxford University Press (OUP). - 1674-2788 .- 1759-4685. ; 11:5, s. 356-370
- Relaterad länk:
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https://academic.oup...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- The muscle RING-finger protein-1 (MuRF1) is an E3 ubiquitin ligase expressed in skeletal and cardiac muscle tissues and it plays important roles in muscle remodeling. Upregulation of MuRF1 gene transcription participates in skeletal muscle atrophy, on contrary downregulation of protein expression leads to cardiac hypertrophy. MuRF1 gene point mutations have been found to generate protein aggregate myopathies defined as muscle disorder characterized by protein accumulation in muscle fibers. We have discovered that MuRF1 turned out to be also a target for a new post-translational modification arbitrated by conjugation of SUMO1 and it is mediated by the SUMO ligases E2 UBC9 and the E3 PIASγ/4. SUMOylation takes place at lysine 238 localized at the second coiled-coil protein domain that is required for efficient substrate interaction for polyubiquitination. We provided evidence that SUMOylation is essential for MuRF1 nuclear translocation and its mitochondria accumulation is enhanced in hyperglycemic conditions delivering a stabilization of the overall SUMOylated proteins in cultured myocytes. Thus, our findings add this SUMO1 post-translational modification as a new concept to understand muscle disorders related to the defect in MuRF1 activity.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Physiology (hsv//eng)
Nyckelord
- TRIM 63 /MuRF 1
- muscle remodeling
- SUMO
- protein degradation
- hyperglycemia
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Heras, Gabriel
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Namuduri, Arvind ...
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Traini, Leonardo
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Shevchenko, Gann ...
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Falk, Alexander, ...
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Bergström Lind, ...
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visa fler...
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Mi, Jia
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Tian, Geng
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Gastaldello, Ste ...
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Uppsala universitet
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Karolinska Institutet