Transportin-1-dependent YB-1 nuclear import

Biochem Biophys Res Commun. 2016 Nov 25;480(4):629-634. doi: 10.1016/j.bbrc.2016.10.107. Epub 2016 Oct 26.

Abstract

The DNA/RNA-binding protein YB-1 (Y-box binding protein 1) performs multiple functions both in the cytoplasm and the nucleus of the cell. Generally localized to the cytoplasm, under certain conditions YB-1 is translocated to the nucleus. Here we report for the first time a transport factor that mediates YB-1 nuclear import - transportin-1. The YB-1/transportin-1 complex can be isolated from HeLa cell extract. Nuclear import of YB-1 and its truncated form YB-1 (1-219) in in vitro transport assay was diminished in the presence of a competitor substrate and ceased in the presence of transportin-1 inhibitor M9M. Inhibitors of importin β1 had no effect on YB-1 transport. Furthermore, transport of YB-1 (P201A/Y202A) and YB-1 (1-219) (P201A/Y202A) bearing inactivating mutations in the transportin-1-dependent nuclear localization signal was practically abolished. Together, these results indicate that transportin-1 mediates YB-1 nuclear translocation.

Keywords: Nuclear import; Transportin-1; YB-1.

MeSH terms

  • Active Transport, Cell Nucleus / physiology
  • Binding Sites
  • Cell Nucleus / metabolism*
  • HeLa Cells
  • Humans
  • Protein Binding
  • Y-Box-Binding Protein 1 / chemistry
  • Y-Box-Binding Protein 1 / metabolism*
  • beta Karyopherins / chemistry
  • beta Karyopherins / metabolism*

Substances

  • TNPO1 protein, human
  • Y-Box-Binding Protein 1
  • beta Karyopherins