Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.

By V. Bernier-Villamor, Deborah A. Sampson, M. Matunis, C. Lima. Cell, 2002

600 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/db9ae53f3327193000033a2c7b3416b8c1336735

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Citations in the corpus

Ubiquitin: structures, functions, mechanisms. (2004, background): “These interactions are known to contribute significantly to the Ubc9/RanGAP1 binding affinity [52] and should apply in all sumoylation reactions involving a consensus site, as suggested by biochemical studies with two other substrates [51].”
Modification of proteins by ubiquitin and ubiquitin-like proteins. (2006, background): “Insights into E3 ligase activity revealed by a SUMO-RanGAP1Ubc9-Nup358 complex.”
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO (2002, background): “The SUMO-conjugating enzyme UBC9 usually binds substrates directl”
Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, background): “In vitro experiments have shown that high concentration of Ubc9 and the E1 enzy e is often sufficient to SUMOylate a substrate protein [98,99].”
Concepts in sumoylation: a decade on (2007, background): “The SUMO family SUMO proteins are ∼10 kD in size and resemble the three-dimensional structure of ubiquiti”
SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? (2004, background): “Consistent with structural studies showing direct recognition of this consensus motif by the Ubc9 active site, recombinant E1, E2, and SUMO are sufficient for ATP-dependent SUMO modification of substrates in vitro (Bernier-Villamor et al. 2002).”
Abiotic stress response in plants : when post-transcriptional and post-translational regulations control transcription (2008, background): “E2 can directly bind and sumoylate substrates in vitro by recognising the consensus motif CKxE/ D (C: hydrophobic amino acid; K: SUMO target lysine; D/E acidic amino acids) [102,103].”
Sumoylation: a regulatory protein modification in health and disease. (2013, background): “This motif must be part of an extended structure to be recognized by Ubc9 (31, 115).”