Nuclear transport factor directs localization of protein synthesis during mitosis

Nat Cell Biol. 2009 Mar;11(3):350-6. doi: 10.1038/ncb1844. Epub 2009 Feb 8.


Export of messenger RNA from the transcription site in the nucleus and mRNA targeting to the translation site in the cytoplasm are key regulatory processes in protein synthesis. In yeast, the mRNA-binding proteins Nab2p and Nab4p/Hrp1p accompany transcripts to their translation site, where the karyopherin Kap104p mediates both their dissociation from the mRNA and their transport back into the nucleus. We found that Kap104p localized to the distal bud tip and the bud neck during cell division, resulting in a localized release of translation-competent mRNA and increased protein synthesis in the emerging daughter cell. Temporally and spatially coordinated localization of Kap104p is a new mechanism for the asymmetric distribution of protein synthesis in dividing cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Cell Nucleus / metabolism*
  • Cytoplasm / metabolism
  • Gene Expression Regulation, Fungal
  • Karyopherins / genetics
  • Karyopherins / metabolism*
  • Mitosis*
  • Models, Biological
  • Nucleocytoplasmic Transport Proteins / metabolism
  • Protein Biosynthesis*
  • Protein Transport
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA-Binding Proteins / metabolism
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • beta Karyopherins


  • KAP104 protein, S cerevisiae
  • Karyopherins
  • NAB2 protein, S cerevisiae
  • Nucleocytoplasmic Transport Proteins
  • RNA, Messenger
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae Proteins
  • beta Karyopherins