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- Title
A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity.
- Authors
Merrill, Jacqueline C; Melhuish, Tiffany A; Kagey, Michael H; Yang, Shen-Hsi; Sharrocks, Andrew D; Wotton, David
- Abstract
Modification of proteins by the small ubiquitin like modifier (SUMO) is an essential process in mammalian cells. SUMO is covalently attached to lysines in target proteins via an enzymatic cascade which consists of E1 and E2, SUMO activating and conjugating enzymes. There is also a variable requirement for non-enzymatic E3 adapter like proteins, which can increase the efficiency and specificity of the sumoylation process. In addition to covalent attachment of SUMO to target proteins, specific non-covalent SUMO interaction motifs (SIMs) that are generally short hydrophobic peptide motifs have been identified.
- Publication
PloS one, 2010, Vol 5, Issue 1, pe8794
- ISSN
1932-6203
- Publication type
Journal Article
- DOI
10.1371/journal.pone.0008794