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Molecular and Cellular Biology, September 1999, p. 6276-6285, Vol. 19, No. 9
Departments of Gene
Expression1 and Biochemical
Instrumentation,3 European Molecular
Biology Laboratory,
Received 22 March 1999/Returned for modification 5 May
1999/Accepted 21 June 1999
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.
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
RanGTP-Regulated Interactions of CRM1 with
Nucleoporins and a Shuttling DEAD-Box Helicase
*
Corresponding author. Mailing address: EMBL
Gene
Expression, Meyerhofstrasse 1, 69117 Heidelberg, Germany. Phone:
49-6221-387317. Fax: 49-6221-387518. E-mail:
mattaj{at}embl-heidelberg.de.
Molecular and Cellular Biology, September 1999, p. 6276-6285, Vol. 19, No. 9
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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