Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.
By Jing Song, L. Durrin, T. A. Wilkinson, T. Krontiris, Yuan Chen. Proceedings of the National Academy of Sciences of the United States of America, 2004
605 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology, Parasitology
View Paper: https://www.semanticscholar.org/paper/fcd91a17dfeb553dcd9cb9b98483fe6be333b34a
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Citations in the corpus
- Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins (2007, background): “A conserved bstrand on SUMO is key to mediating its interaction with the SIM (see Introduction), with its residues being involved in van der Waal’s contacts with the hydrophobic residues in SIM (Song et al, 2004, 2005; Hecker et al, 2006).”
- GPS-SUMO: a tool for the prediction of sumoylation sites and SUMO-interaction motifs (2014, background): “refuted the dominant role of serine residue in the SIMs (20), and discovered a new hydrophobic core motif of [VI]X[VI][VI] as a bona fide SIM (21).”
- Smad transcription factors. (2005, background): “The rising interest in the ubiquitin-like modification involving SUMO (small ubiquitin-like modifier) has shown that sumoylation alters protein function by creating a composite interaction domain (Song et al. 2004).”
- RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation (2008, neutral): “d c RNF4 WT mtSIM1 mtSIM2 mtSIM3 mtSIM4 mtSIM1,2 mtSIM1,2,3 mtSIM1,2,3,4 ∆N(1-20) ∆1(31-65) ∆2(66-98) ∆3(99-118) CS1 CS2 SIMs RING”
- Modification of proteins by ubiquitin and ubiquitin-like proteins. (2006, background): “Subsequent structural and mutational characterization of peptides that bind SUMO suggested the consensus sequence V/I-X-V/IV/I, where X is any amino acid (Song et al. 2004).”