Abstract
SUMO (small ubiquitin-related modifier) is a ubiquitin-like family member that is conjugated to its substrates through discrete enzymatic steps: activation, involving the E1 enzyme [SAE (SUMO-activating enzyme) 1-SAE2], conjugation, involving the E2 enzyme [Ubc9 (ubiquitin-conjugating enzyme 9)], and substrate modification, through the co-operation of Ubc9 and E3 protein ligases. Work from our laboratory has shown the first example of a viral protein, Gam1, that binds to the E1 heterodimer, inhibiting its function and causing a complete block of the SUMOylation pathway both in vivo and in vitro, followed by SAE1-SAE2 degradation. The mechanism by which a viral protein inactivates and subsequently degrades an essential cellular enzyme, arresting a key regulatory pathway, will be discussed. Although four distinct SUMO isoforms have been described, I will use SUMO to describe the entire system.
Original language | English |
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Pages (from-to) | 1419-1421 |
Number of pages | 3 |
Journal | Biochemical Society Transactions |
Volume | 35 |
Issue number | 6 |
DOIs | |
Publication status | Published - Dec 2007 |
Keywords
- E1 activating enzyme
- Elongin (Elo)
- Gam1
- Small ubiquitin-related modifier (SUMO)
- SUMOylation
- Viral protein
ASJC Scopus subject areas
- Biochemistry