Nuclear translocation of the Y-box binding protein by ultraviolet irradiation

Abstract

The Y-box binding protein, YB-1, is a member of a DNA binding protein family with a structurally and functionally conserved cold shock domain. Using Western blotting and immunohistochemical methods, larger amounts of YB-1 were detected in the cytosol, particularly at the perinuclear region, than in the nucleus of human cancer cells. UV irradiation increased accumulation of YB-1 in the nucleus at 20 min and thereafter. This translocation of YB-1 into the nucleus by UV irradiation was blocked by the protein kinase inhibitor H-7, but not HA-1004. Both green fluorescent protein (GFP)-YB-1 and GFP-YB-1C with the C-terminus (248-317) of YB-1 were located mainly in the cytosol, but GFP-YB-1deltaC with a deletion at the C-terminus of YB-1 was located in the nucleus. YB-1 is translocated into the nucleus by UV irradiation, possibly through a protein kinase C-mediated signal transduction pathway, and the C-terminal region of YB-1 might be important for cytoplasmic retention of YB-1.