Nuclear localization signals for four distinct Karyopherin-β nuclear import systems

Michael Soniat, Yuh Min Chook

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

The Karyopherin-β family of proteins mediates nuclear transport of macromolecules. Nuclear versus cytoplasmic localization of proteins is often suggested by the presence of NLSs (nuclear localization signals) or NESs (nuclear export signals). Import-Karyopherin-βs or Importins bind to NLSs in their protein cargos to transport them through nuclear pore complexes into the nucleus. Until recently, only two classes of NLS had been biochemically and structurally characterized: the classical NLS, which is recognized by the Importin-α/β heterodimer and the PY-NLS (proline-tyrosine NLS), which is recognized by Karyopherin-β2 or Transportin-1. Structures of two other Karyopherin-βs, Kap121 and Transportin-SR2, in complex with their respective cargos were reported for the first time recently, revealing two new distinct classes of NLSs. The present paper briefly describes the classical NLS, reviews recent literature on the PY-NLS and provides in-depth reviews of the two newly discovered classes of NLSs that bind Kap121p and Transportin-SR respectively.

Original languageEnglish (US)
Pages (from-to)353-362
Number of pages10
JournalBiochemical Journal
Volume468
Issue number3
DOIs
StatePublished - Jun 15 2015

Fingerprint

Karyopherins
Nuclear Localization Signals
Cell Nucleus Active Transport
Proline
Tyrosine
Nuclear Export Signals
Nuclear Pore
Proteins
Nuclear Proteins
Macromolecules

Keywords

  • Importin
  • Karyopherin
  • Nuclear import
  • Nuclear localization signal (NLS)
  • Nuclear pore
  • Nucleocytoplasmic transport

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Nuclear localization signals for four distinct Karyopherin-β nuclear import systems. / Soniat, Michael; Chook, Yuh Min.

In: Biochemical Journal, Vol. 468, No. 3, 15.06.2015, p. 353-362.

Research output: Contribution to journalArticle

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