Mechanistic insights from the recent structures of the CRM1 nuclear export complex and its disassembly intermediate

Masako Koyama, Yoshiyuki Matsuura

Research output: Contribution to journalReview article

4 Citations (Scopus)

Abstract

CRM1 (also known as exportin 1 or Xpo1) is the most versatile nuclear export receptor (exportin) that carries a broad range of proteins and ribonucleoproteins from the nucleus to the cytoplasm through the nuclear pore complex. The majority of the export substrates of CRM1 contain a short peptide sequence, so-called leucine-rich nuclear export signal (NES), which typically harbor four or five characteristically spaced hydrophobic residues. The transport directionality is determined by the small GTPase Ran and Ran-binding proteins that control the binding and dissociation of cargo. Here we review recent structural studies that advanced understanding of how NES is specifically recognized by CRM1 in the nucleus, and how NES is rapidly dissociated from CRM1 in the cytoplasm.

Original languageEnglish
Pages (from-to)145-150
Number of pages6
JournalBiophysics (Japan)
Volume8
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • CRM1
  • Nuclear export signal
  • Nuclear pore
  • Ran
  • RanBP1

ASJC Scopus subject areas

  • Biophysics

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