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Modification of ran GTPase-activating protein by the small ubiquitin-related modifier SUMO-1 requires Ubc9, an E2-type ubiquitin-conjugating enzyme homologue

Covalent modification of the Ran GTPase-activating protein RanGAP1 with the ubiquitin-related protein SUMO-1 promotes its association with Nup358, a component of the cytoplasmic fibrils emanating from the nuclear pore complex (1, 2). in Xenopus egg extracts, Nup358 can be found in a complex with Ubc...

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Bibliographic Details
Main Authors: Lee, Gene W. (Author) , Melchior, Frauke (Author) , Matunis, Michael J. (Author) , Mahajan, Rohit (Author) , Tian, Qingsheng (Author) , Anderson, Paul (Author)
Format: Article (Journal)
Language:English
Published: 13 March 1998
In: The journal of biological chemistry
Year: 1998, Volume: 273, Issue: 11, Pages: 6503-6507
ISSN:1083-351X
DOI:10.1074/jbc.273.11.6503
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1074/jbc.273.11.6503
Verlag, kostenfrei, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925818677737
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Author Notes:Gene W. Lee, Frauke Melchior, Michael J. Matunis, Rohit Mahajan, Qingsheng Tian, and Paul Anderson
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Summary:Covalent modification of the Ran GTPase-activating protein RanGAP1 with the ubiquitin-related protein SUMO-1 promotes its association with Nup358, a component of the cytoplasmic fibrils emanating from the nuclear pore complex (1, 2). in Xenopus egg extracts, Nup358 can be found in a complex with Ubc9 (3), a structural homologue of the E2-type ubiquitin-conjugating enzymes (UBCs). Here we show that a subset of the human homologue of Ubc9 (HsUbc9) colocalizes with RanGAP1 at the nuclear envelope. HsUbc9 forms thiolester conjugates with recombinant SUMO-1, but not with recombinant ubiquitin, indicating that it is functionally distinct from E2-type UBCs. Finally, HsUbc9 is required for the modification of RanGAP1 by SUMO-1. These results suggest that HsUbc9 is a component of a novel enzymatic cascade that modifies RanGAP1, and possibly other substrates, with SUMO-1.
Item Description:Gesehen am 06.09.2023
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.273.11.6503

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