Ubiquitin-dependent degradation of TGF-β-activated Smad2 Journal Article
| Authors: | Lo, R. S.; Massagué, J. |
| Article Title: | Ubiquitin-dependent degradation of TGF-β-activated Smad2 |
| Abstract: | SMAD proteins are phosphorylated by transforming growth factor-β (TGF-β) receptors and translocate to the nucleus, where they control transcription. Here we investigate the fate of activated Smad2. We show that receptormediated activation leads to multi-ubiquitination and subsequent degradation of Smad2 by the proteasome. Ubiquitination of Smad2 is a consequence of its accumulation in the nucleus. If degradation is averted, the phosphorylated Smad2 remains in the nucleus in an active state. By targeting Smad2 for destruction, TGF-β ensures the irreversible termination of its own signalling function. |
| Keywords: | signal transduction; dna binding protein; genetics; dna-binding proteins; ubiquitin; animal; metabolism; animals; proteasome; proteasome endopeptidase complex; biological model; models, biological; smad2 protein; transforming growth factor beta; cell line; drug effect; enzymology; transfection; phosphorylation; fluorescent antibody technique; drug antagonism; protein processing; protein processing, post-translational; genetic transfection; transactivator protein; trans-activators; cell nucleus; multienzyme complex; multienzyme complexes; half life time; half-life; ubiquitins; cysteine proteinase; cysteine endopeptidases; humans; human; article; smad2 protein, human |
| Journal Title: | Nature Cell Biology |
| Volume: | 1 |
| Issue: | 8 |
| ISSN: | 1465-7392 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1999-12-01 |
| Start Page: | 472 |
| End Page: | 478 |
| Language: | English |
| PUBMED: | 10587642 |
| PROVIDER: | scopus |
| DOI: | 10.1038/70258 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
