Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export

Mark E. Lindsay, James M. Holaska, Katie Welch, Bryce M. Paschal, Ian G. Macara

Research output: Contribution to journalArticlepeer-review

113 Scopus citations

Abstract

Crm1 is a member of the karyopherin family of nucleocytoplasmic transport receptors and mediates the export of proteins from the nucleus by forming a ternary complex with cargo and Ran:GTP. This complex translocates through the nuclear pores and dissociates in the cytosol. The yeast protein Yrb2p participates in this pathway and binds Crm1, but its mechanism of action has not been established. We show that the human orthologue of Yrb2p, Ran-binding protein 3 (RanBP3), acts as a cofactor for Crm1-mediated export in a permeabilized cell assay. RanBP3 binds directly to Crm1, and the complex posseses an enhanced affinity for both Ran:GTP and cargo, RanBP3 shuttles between the nucleus and the cytoplasm by a Crm1-dependent mechanism, and the Crm1-RanBP3-NES-Ran:GTP quarternary complex can associate with nucleoporins. We infer that this complex translocates through the nuclear pore to the cytoplasm where it is disassembled by RanBP1 and Ran GTPase-activating protein.

Original languageEnglish (US)
Pages (from-to)1391-1402
Number of pages12
JournalJournal of Cell Biology
Volume153
Issue number7
DOIs
StatePublished - Jun 26 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology

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