We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase
- Authors
Jogo, Misako; Shiraishi, Seiji; Tamura, Taka-aki
- Abstract
Abstract: Myogenesis is conducted by transcription factors including MyoD and myogenin. Myogenin is known to be polyubiquitinated by SCF (Skp1/Cullin 1/F-box protein) followed by proteasomal degradation, though the participating F-box protein is remaining unidentified. In this study, we found that myogenin in differentiated myoblasts is destabilized by muscle atrophy-inducing dexamethasone and that MAFbx (muscle atrophy F-box protein) is increased in atrophying myotubes. MAFbx overexpression resulted in MG132-sensitive reduction of myogenin. Myogenin had a MAFbx-recognition motif and interacted with MAFbx. MAFbx activated polyubiquitination of myogenin. The results of this study suggest that MAFbx functions as an F-box protein for ubiquitination of myogenin. Structured summary: MINT-7222713: Myogenin (uniprotkb:P12979) physically interacts (MI:0914) with MAFbx (uniprotkb:Q9CPU7) by anti tag coimmunoprecipitation (MI:0007) MINT-7222741: Myogenin (uniprotkb:P12979) physically interacts (MI:0914) with MAFbx (uniprotkb:Q9CPU7) by anti bait coimmunoprecipitation (MI:0006) MINT-7222726: Myogenin (uniprotkb:P12979) and MAFbx (uniprotkb:Q9CPU7) colocalize (MI:0403) by fluorescence microscopy (MI:0416) MINT-7222760: Myogenin (uniprotkb:P12979) physically interacts (MI:0914) with Ubiquitin (uniprotkb:P62991) by anti bait coimmunoprecipitation (MI:0006)
- Subjects
LIGASES; MYOGENESIS; TRANSCRIPTION factors; PROTEINS; MYOBLASTS; CELL differentiation; FLUORESCENCE microscopy
- Publication
FEBS Letters, 2009, Vol 583, Issue 17, p2715
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.07.033