A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
We have found that the mammalian Ran GTPase-activating protein RanGAP1 is highly concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it associates with the 358-kDa Ran-GTP-binding protein RanBP2. This interaction requires the ATP-dependent posttranslational conjugation...
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| Main Authors: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
10 January 1997
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| In: |
Cell
Year: 1997, Volume: 88, Issue: 1, Pages: 97-107 |
| ISSN: | 1097-4172 |
| DOI: | 10.1016/S0092-8674(00)81862-0 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/S0092-8674(00)81862-0 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0092867400818620 
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| Author Notes: | Rohit Mahajan, Christian Delphin, Tinglu Guan, Larry Gerace, and Frauke Melchior |
| Summary: | We have found that the mammalian Ran GTPase-activating protein RanGAP1 is highly concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it associates with the 358-kDa Ran-GTP-binding protein RanBP2. This interaction requires the ATP-dependent posttranslational conjugation of RanGAP1 with SUMO-1 (for small ubiquitin-related modifier), a novel protein of 101 amino acids that contains low but significant homology to ubiquitin. SUMO-1 appears to represent the prototype for a novel family of ubiquitin-related protein modifiers. Inhibition of nuclear protein import resulting from antibodies directed at NPC-associated RanGAP1 cannot be overcome by soluble cytosolic RanGAP1, indicating that GTP hydrolysis by Ran at RanBP2 is required for nuclear protein import. |
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| Item Description: | Gesehen am 13.03.2023 |
| Physical Description: | Online Resource |
| ISSN: | 1097-4172 |
| DOI: | 10.1016/S0092-8674(00)81862-0 |