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Protein modification by SUMO, a small ubiquitin‐like modifier
Author(s) -
Lima Christopher D
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a207-d
Subject(s) - ubiquitin , ubiquitin protein ligases , proteases , ubiquitin conjugating enzyme , enzyme , biochemistry , protease , lysine , proteolysis , deubiquitinating enzyme , chemistry , substrate specificity , ubiquitin ligase , microbiology and biotechnology , biology , amino acid , gene
Ubiquitin (Ub) and ubiquitin‐like (Ubl) pathways utilize distinct enzymes to activate Ub/Ubl modifiers for conjugation to protein substrate lysine residues. We are characterizing the biochemical and structural properties for enzymes and substrates in the SUMO pathway (small ubiquitin‐like modifier), including SUMO proteases, the E1 activating enzyme, the E2 conjugating protein, and E3 ligases. E2 conjugating proteins and E3 ligases ensure specificity and enhance conjugation in Ub/Ubl pathways. Several SUMO E3s have been identified to date that include a unique class of RING‐type E3s and E3s unrelated to either HECT or RING E3 families. Recent work has focused on characterization of E2‐ and E3‐mediated conjugation and SUMO protease activities, the results of which will be discussed. Supported in part by a grant from the National Institutes of Health (GM65872) and the Rita Allan Foundation (C.D.L.)