A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

被引:977
|
作者
Mahajan, R
Delphin, C
Guan, TL
Gerace, L
Melchior, F
机构
[1] Department of Cell Biology, Scripps Research Institute, San Diego, CA 92037
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0092-8674(00)81862-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页码:97 / 107
页数:11
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