Nuclear import by karyopherin-βs: Recognition and inhibition

Yuh Min Chook, Katherine E. Süel

Research output: Contribution to journalReview articlepeer-review

304 Scopus citations


Proteins in the karyopherin-β family mediate the majority of macromolecular transport between the nucleus and the cytoplasm. Eleven of the 19 known human karyopherin-βs and 10 of the 14. S. cerevisiae karyopherin-βs mediate nuclear import through recognition of nuclear localization signals or NLSs in their cargos. This receptor-mediated process is essential to cellular viability as proteins are translated in the cytoplasm but many have functional roles in the nucleus. Many known karyopherin-β-cargo interactions were discovered through studies of the individual cargos rather than the karyopherins, and this information is thus widely scattered in the literature. We consolidate information about cargos that are directly recognized by import-karyopherin-βs and review common characteristics or lack thereof among cargos of different import pathways. Knowledge of karyopherin-β-cargo interactions is also critical for the development of nuclear import inhibitors and the understanding of their mechanisms of inhibition. This article is part of a Special Issue entitled: Regulation of Signaling and Cellular Fate through Modulation of Nuclear Protein Import.

Original languageEnglish (US)
Pages (from-to)1593-1606
Number of pages14
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number9
StatePublished - Sep 2011


  • Classical-NLS
  • Importin
  • Karyopherin
  • NLS
  • Nuclear import
  • Nuclear localization
  • Nuclear localization signal
  • Nuclear pore complex
  • PY-NLS
  • Transportin

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Nuclear import by karyopherin-βs: Recognition and inhibition'. Together they form a unique fingerprint.

Cite this