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

Masako Koyama, Yoshiyuki Matsuura*

*この研究の対応する著者

研究成果: Review article査読

6 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)145-150
ページ数6
ジャーナルBiophysics (Japan)
8
DOI
出版ステータスPublished - 2012
外部発表はい

ASJC Scopus subject areas

  • 生物理学

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