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Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase.

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.
AuthorsMisako Jogo, Seiji Shiraishi, Taka-aki Tamura
JournalFEBS letters (FEBS Lett) Vol. 583 Issue 17 Pg. 2715-9 (Sep 03 2009) ISSN: 1873-3468 [Electronic] England
PMID19631210 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Glucocorticoids
  • Muscle Proteins
  • Myog protein, mouse
  • Myogenin
  • Recombinant Fusion Proteins
  • Insulin-Like Growth Factor I
  • Dexamethasone
  • Fbxo32 protein, mouse
  • SKP Cullin F-Box Protein Ligases
Topics
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Dexamethasone (metabolism)
  • Glucocorticoids (metabolism)
  • Insulin-Like Growth Factor I (metabolism)
  • Mice
  • Molecular Sequence Data
  • Muscle Proteins (genetics, metabolism)
  • Myoblasts (cytology, physiology)
  • Myogenin (genetics, metabolism)
  • RNA Interference
  • Recombinant Fusion Proteins (genetics, metabolism)
  • SKP Cullin F-Box Protein Ligases (genetics, metabolism)

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