Regulation of TGF-β signal transduction by mono- and deubiquitylation of Smads

Sirio Dupont, Masafumi Inui, Stuart Newfeld

Research output: Contribution to journalReview articlepeer-review

29 Scopus citations

Abstract

Polyubiquitylation leading to proteasomal degradation is a well-established mechanism for regulating TGF-β signal transduction components such as receptors and Smads. Recently, an equally important role was suggested for monoubiquitylation of both Smad4 and receptor-associated Smads that regulates their function without protein degradation. Monoubiquitylation of Smads was discovered following the identification of deubiquitylases required for TGF-β signaling, suggesting that continuous cycles of Smad mono- and deubiquitylation are required for proper TGF-β signal transduction. Here we summarize and discuss recent work on Smad mono- and deubiquitylation.

Original languageEnglish (US)
Pages (from-to)1913-1920
Number of pages8
JournalFEBS Letters
Volume586
Issue number14
DOIs
StatePublished - Jul 4 2012

Keywords

  • BMP
  • Ectodermin/Tif1-γ/Trim33
  • Fat facets/Fam/Usp9X
  • Smad4/Medea
  • Usp15

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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