RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase

Peter Askjaer, Angela Bachi, Matthias Wilm, F. Ralf Bischoff, Daniel L. Weeks, Vera Ogniewski, Mutsuhito Ohno, Christof Niehrs, Jørgen Kjems, Iain W. Mattaj*, Maarten Fornerod

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

180 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)6276-6285
Number of pages10
JournalMolecular and Cellular Biology
Issue number9
Publication statusPublished - Sept 1999


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