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 language | English (US) |
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Pages (from-to) | 1913-1920 |
Number of pages | 8 |
Journal | FEBS Letters |
Volume | 586 |
Issue number | 14 |
DOIs | |
State | Published - 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