RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import.
RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import.
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DOI：
10.1083/jcb.135.3.559
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发表时间：
1996-11
影响因子：
7.8
通讯作者：
Adam, SA
中科院分区：
文献类型：
--
作者：
Chi, NC;Adam, EJH;Visser, GD;Adam, SA
在渗透细胞试验中，已经确定了三个重建核蛋白进口的因素：NLS受体、p97和Ran/TC4。Ran/TC4反过来又与许多参与GTP水解调控或作为核孔组分的蛋白质相互作用。凝胶过滤层析分离的HeLa细胞提取物经免疫吸附证实，RanBP1和RanBP2两种ran结合蛋白与p97形成离散的复合物。> 400-kD复合物包含p97、Ran和RanBP2。另一个150- 300 kD的复合物由p97、Ran和RanBP1组成。第二种三聚体可以由重组蛋白重组而成。在溶液结合实验中，Ran-GTP与p97有高亲和力结合，但未检测到Ran-GDP与p97的结合。RanBP1与Ran- gdp或Ran- gtp的结合将两种形式的Ran对p97的亲和力提高到相同水平。Ran-GTP与p97的结合使p97与固定的NLS受体分离，而Ran-GDP/RanBP1/p97复合物不与受体分离。在洋地黄苷渗透细胞对接实验中，RanBP1稳定受体复合物，防止温度依赖性的孔释放。当加入重组NLS受体、p97和Ran-GDP的进口试验时，RanBP1显著刺激运输。这些结果表明，RanBP1通过稳定Ran-GDP与p97的相互作用，促进了核蛋白进口的对接和转运步骤。
Three factors have been identified that reconstitute nuclear protein import in a permeabilized cell assay: the NLS receptor, p97, and Ran/TC4. Ran/TC4, in turn, interacts with a number of proteins that are involved in the regulation of GTP hydrolysis or are components of the nuclear pore. Two Ran-binding proteins, RanBP1 and RanBP2, form discrete complexes with p97 as demonstrated by immunoadsorption from HeLa cell extracts fractionated by gel filtration chromatography. A > 400-kD complex contains p97, Ran, and RanBP2. Another complex of 150- 300 kD was comprised of p97, Ran, and RanBP1. This second trimeric complex could be reconstituted from recombinant proteins. In solution binding assays, Ran-GTP bound p97 with high affinity, but the binding of Ran-GDP to p97 was undetectable. The addition of RanBP1 with Ran-GDP or Ran-GTP increased the affinity of both forms of Ran for p97 to the same level. Binding of Ran-GTP to p97 dissociated p97 from immobilized NLS receptor while the Ran-GDP/RanBP1/p97 complex did not dissociate from the receptor. In a digitonin-permeabilized cell docking assay, RanBP1 stabilizes the receptor complex against temperature-dependent release from the pore. When added to an import assay with recombinant NLS receptor, p97 and Ran-GDP, RanBP1 significantly stimulates transport. These results suggest that RanBP1 promotes both the docking and translocation steps in nuclear protein import by stabilizing the interaction of Ran-GDP with p97.
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DOI：
10.1083/jcb.130.5.1017
发表时间：
1995-09
期刊：
The Journal of cell biology
影响因子：
--
作者：
Corbett AH;Koepp DM;Schlenstedt G;Lee MS;Hopper AK;Silver PA
通讯作者：
Silver PA
DOI：
10.1073/pnas.92.8.3328
发表时间：
1995-04-11
影响因子：
11.1
作者：
BEDDOW, AL;RICHARDS, SA;MACARA, IG
通讯作者：
MACARA, IG
核孔NUP116P的GLFG重复区域与KAP95P相互作用，KAP95P是必不可少的酵母核进口因子。
影响因子：
7.8
作者：
Iovine, M K;Watkins, J L;Wente, S R
通讯作者：
Wente, S R
DOI：
10.1073/pnas.88.23.10830
发表时间：
1991-12-01
影响因子：
11.1
作者：
BISCHOFF, FR;PONSTINGL, H
通讯作者：
PONSTINGL, H
DOI：
10.1073/pnas.92.16.7525
发表时间：
1995-08-01
影响因子：
11.1
作者：
DINGWALL, C;KANDELSLEWIS, S;SERAPHIN, B
通讯作者：
SERAPHIN, B