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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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Hauptverfasser: Mahajan, Rohit (VerfasserIn) , Delphin, Christian (VerfasserIn) , Guan, Tinglu (VerfasserIn) , Gerace, Larry (VerfasserIn) , Melchior, Frauke (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 10 January 1997
In: Cell
Year: 1997, Jahrgang: 88, Heft: 1, Pages: 97-107
ISSN:1097-4172
DOI:10.1016/S0092-8674(00)81862-0
Online-Zugang: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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Verfasserangaben:Rohit Mahajan, Christian Delphin, Tinglu Guan, Larry Gerace, and Frauke Melchior

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520 |a 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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