Abstract
Although the post-translational modification of proteins with small ubiquitin-like modifier (SUMO) has a role in many biological processes, it was thought that SUMO, unlike ubiquitin, does not target proteins for degradation. However, these views need to be revised, as recent findings in yeast and human cells indicate that SUMO can act as a signal for the recruitment of E3 ubiquitin ligases, which leads to the ubiquitylation and degradation of the modified protein.
Original language | English |
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Pages (from-to) | 564-568 |
Number of pages | 5 |
Journal | Nature Reviews Molecular Cell Biology |
Volume | 10 |
Issue number | 8 |
DOIs | |
Publication status | Published - Aug 2009 |
Keywords
- ACUTE PROMYELOCYTIC LEUKEMIA
- TRIOXIDE-INDUCED APOPTOSIS
- NUCLEAR-PORE COMPLEX
- RAR-ALPHA
- SACCHAROMYCES-CEREVISIAE
- IN-VITRO
- PML
- PROTEIN
- RNF4
- LIGASE