Recognition of nuclear targeting signals by Karyopherin-β proteins

Darui Xu, Alicia Farmer, Yuh Min Chook

Research output: Contribution to journalReview articlepeer-review

173 Scopus citations

Abstract

The Karyopherin-β family of nuclear transport factors mediates the majority of nucleocytoplasmic transport. Although each of the 19 Karyopherin-βs transports unique sets of cargos, only three classes of nuclear localization and export signals, or NLSs and NESs, have been characterized. The short basic classical-NLS was first discovered in the 1980s and their karyopherin-bound structures were first reported more than 10 years ago. More recently, structural and biophysical studies of Karyopherin-β2-cargo complexes led to definition of the complex and diverse PY-NLS. Structural knowledge of the leucine-rich NES is finally available more than 10 years after the discovery of its recognition by the exportin CRM1. We review recent findings relating to how these three classes of nuclear targeting signals are recognized by their Karyopherin-β nuclear transport factors.

Original languageEnglish (US)
Pages (from-to)782-790
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume20
Issue number6
DOIs
StatePublished - Dec 2010

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Recognition of nuclear targeting signals by Karyopherin-β proteins'. Together they form a unique fingerprint.

Cite this