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XB-ART-12485
Mol Cell Biol 1999 Sep 01;199:6276-85. doi: 10.1128/MCB.19.9.6276.
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RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase.

Askjaer P , Bachi A , Wilm M , Bischoff FR , Weeks DL , Ogniewski V , Ohno M , Niehrs C , Kjems J , Mattaj IW , Fornerod M .


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CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP. Using a quantitative CRM1-NES cargo binding assay, significant differences in affinity for CRM1 among natural NESs are demonstrated, suggesting that the steady-state nucleocytoplasmic distribution of shuttling proteins could be determined by the relative strengths of their NESs. We also show that a trimeric CRM1-NES-RanGTP complex is disassembled by RanBP1 in the presence of RanGAP, even though RanBP1 itself contains a leucine-rich NES. Selection of CRM1-binding proteins from Xenopus egg extract leads to the identification of an NES-containing DEAD-box helicase, An3, that continuously shuttles between the nucleus and the cytoplasm. In addition, we identify the Xenopus homologue of the nucleoporin CAN/Nup214 as a RanGTP- and NES cargo-specific binding site for CRM1, suggesting that this nucleoporin plays a role in export complex disassembly and/or CRM1 recycling.

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Species referenced: Xenopus
Genes referenced: ddx3x ranbp1 xpo1

References [+] :
Arts, Energy- and temperature-dependent in vitro export of RNA from synthetic nuclei. 1997, Pubmed, Xenbase