Viral control of the SUMO pathway: Gam1, a model system. (23rd November 2007)

• Record Type: Journal Article
• Authors: Chiocca, S.
• Is Part Of: Biochemical Society transactions. Volume 35:Number 6(2007)
• Page Start: 1419
• Page End: 1421
• Publication Date: 2007-11-23
• Subjects: E1 activating enzyme -- elongin (Elo) -- Gam1 -- small ubiquitin-related modifier (SUMO) -- SUMOylation -- viral protein; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0351419
• Languages: English
• ISSNs: 0300-5127

Abstract

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.