Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1- transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are...
AbstractE2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues d...
Sumoylation, the covalent attachment of SUMO (Small Ubiquitin-Like Modifier) to proteins, differs fr...
AbstractE2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues d...
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and ...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and ...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
AbstractPosttranslational modification with SUMO1 regulates protein/protein interactions, localizati...
AbstractA recent paper in Cell shows that the large nucleoporin RanBP2 can act as an E3 enzyme for t...
The conjugation of small ubiquitin-like modifiers SUMO-1, SUMO-2 and SUMO-3 onto target proteins req...
The conjugation of small ubiquitin-like modifiers SUMO-1, SUMO-2 and SUMO-3 onto target proteins req...
AbstractA recent paper in Cell shows that the large nucleoporin RanBP2 can act as an E3 enzyme for t...
AbstractE2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues d...
Sumoylation, the covalent attachment of SUMO (Small Ubiquitin-Like Modifier) to proteins, differs fr...
AbstractE2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues d...
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and ...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and ...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
International audiencePosttranslational modification with SUMO1 regulates protein/protein interactio...
AbstractPosttranslational modification with SUMO1 regulates protein/protein interactions, localizati...
AbstractA recent paper in Cell shows that the large nucleoporin RanBP2 can act as an E3 enzyme for t...
The conjugation of small ubiquitin-like modifiers SUMO-1, SUMO-2 and SUMO-3 onto target proteins req...
The conjugation of small ubiquitin-like modifiers SUMO-1, SUMO-2 and SUMO-3 onto target proteins req...
AbstractA recent paper in Cell shows that the large nucleoporin RanBP2 can act as an E3 enzyme for t...
AbstractE2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues d...
Sumoylation, the covalent attachment of SUMO (Small Ubiquitin-Like Modifier) to proteins, differs fr...
AbstractE2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues d...