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

Fingerprint

Nuclear Export Signals
Cell Nucleus Active Transport
Cytoplasm
ran GTP-Binding Protein
Karyopherins
Nuclear Pore
Ribonucleoproteins
Monomeric GTP-Binding Proteins
Cytoplasmic and Nuclear Receptors
Protein Binding
Leucine
Carrier Proteins
Peptides
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biophysics

Cite this

Mechanistic insights from the recent structures of the CRM1 nuclear export complex and its disassembly intermediate. / Koyama, Masako; Matsuura, Yoshiyuki.

In: Biophysics (Japan), Vol. 8, 2012, p. 145-150.

Research output: Contribution to journalReview article

@article{1a34cb0c77644018bcd877085b6837e0,
title = "Mechanistic insights from the recent structures of the CRM1 nuclear export complex and its disassembly intermediate",
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.",
keywords = "CRM1, Nuclear export signal, Nuclear pore, Ran, RanBP1",
author = "Masako Koyama and Yoshiyuki Matsuura",
year = "2012",
doi = "10.2142/biophysics.8.145",
language = "English",
volume = "8",
pages = "145--150",
journal = "Biophysics (Japan)",
issn = "1349-2942",
publisher = "Biophysical Society of Japan",

}

TY - JOUR

T1 - Mechanistic insights from the recent structures of the CRM1 nuclear export complex and its disassembly intermediate

AU - Koyama, Masako

AU - Matsuura, Yoshiyuki

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - CRM1

KW - Nuclear export signal

KW - Nuclear pore

KW - Ran

KW - RanBP1

UR - http://www.scopus.com/inward/record.url?scp=84870729256&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84870729256&partnerID=8YFLogxK

U2 - 10.2142/biophysics.8.145

DO - 10.2142/biophysics.8.145

M3 - Review article

AN - SCOPUS:84870729256

VL - 8

SP - 145

EP - 150

JO - Biophysics (Japan)

JF - Biophysics (Japan)

SN - 1349-2942

ER -