Transportin-1-dependent YB-1 nuclear import
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 medi...
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Veröffentlicht in: | Biochemical and biophysical research communications 2016-11, Vol.480 (4), p.629-634 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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.
•Transportin-1 mediates YB-1 nuclear import.•YB-1 nuclear translocation is diminished in the presence of transportin-1 inhibitors.•Mutations in the PY motif of YB-1 NLS prevent its translocation to the nucleus. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2016.10.107 |