Abstract
The small ubiquitin-like modifier (SUMO) is covalently linked to a variety of proteins and is deconjugated by SUMO-specific proteases. A characteristic of SUMO modification is that the biological consequences of conjugation do not appear proportionate to the small fraction of substrate that is modified. SUMO conjugation appears to alter the long-term fate of the modified protein even though the SUMO may be rapidly deconjugated. Thus an unmodified protein with a history of SUMO modification may have different properties from a protein that never has been modified. Here, the diverse effects of SUMO modification are discussed and models proposed to explain SUMO actions.
Original language | English |
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Pages (from-to) | 112 |
Number of pages | 12 |
Journal | Molecular Cell |
Volume | 18 |
Publication status | Published - 1 Apr 2005 |
Keywords
- NUCLEAR-PORE COMPLEX
- UBIQUITIN-CONJUGATING ENZYME
- MEDIATED TRANSCRIPTIONAL REPRESSION
- KAPPA-B ACTIVATION
- ANDROGEN RECEPTOR
- PROTEIN SUMO-1
- E3 LIGASE
- SACCHAROMYCES-CEREVISIAE
- SUBSTRATE RECOGNITION
- COVALENT MODIFICATION