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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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
13 March 1998
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| In: |
The journal of biological chemistry
Year: 1998, Jahrgang: 273, Heft: 11, Pages: 6503-6507 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.273.11.6503 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1074/jbc.273.11.6503 Verlag, kostenfrei, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925818677737 |
| Verfasserangaben: | Gene W. Lee, Frauke Melchior, Michael J. Matunis, Rohit Mahajan, Qingsheng Tian, and Paul Anderson |
| Zusammenfassung: | 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. |
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| Beschreibung: | Gesehen am 06.09.2023 |
| Beschreibung: | Online Resource |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.273.11.6503 |