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Structural basis for assembly and disassembly of the CRM1 nuclear export complex.

ABSTRACT: CRM1 (or exportin 1, Xpo1) transports proteins out of the cell nucleus through the nuclear pore complex. In the cytoplasm, GTP hydrolysis and consequent dissociation of Ran from CRM1 releases low-affinity substrates, while additional factors facilitate release of high-affinity substrates. Here we provide a model for human CRM1 export complex assembly and disassembly through structural and biochemical analyses of CRM1 bound to the substrate snurportin 1 (SNUPN, also called snuportin 1).

SUBMITTER: Dong X

PROVIDER: S-EPMC3437629 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature

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Structural basis for assembly and disassembly of the CRM1 nuclear export complex.

Dong Xiuhua X Biswas Anindita A Chook Yuh Min YM

Nature structural & molecular biology 20090401 5

CRM1 (or exportin 1, Xpo1) transports proteins out of the cell nucleus through the nuclear pore complex. In the cytoplasm, GTP hydrolysis and consequent dissociation of Ran from CRM1 releases low-affinity substrates, while additional factors facilitate release of high-affinity substrates. Here we provide a model for human CRM1 export complex assembly and disassembly through structural and biochemical analyses of CRM1 bound to the substrate snurportin 1 (SNUPN, also called snuportin 1). ...[more]

PMID: 19339972

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