SOK1 translocates from the Golgi to the nucleus upon chemical anoxia and induces apoptotic cell death.

SOK1 is a Ste20 protein kinase of the germinal center kinase (GCK) family that has been shown to be activated by oxidant stress and chemical anoxia, a cell culture model of ischemia. More recently, it has been shown to be localized to the Golgi apparatus, where it functions in a signaling pathway required for cell migration and polarization. Herein, we demonstrate that SOK1 regulates cell death after chemical anoxia, as its down-regulation by RNA interference enhances cell survival.

The GCK II and III subfamilies of the STE20 group kinases.

The Ste20 (sterile 20) proteins are a large family of serine/threonine kinases. Since their discovery a growing body of evidence has implicated them in the regulation of signaling pathways governing cell growth, cell differentiation cell death and cell volume. Approximately 30 human members have been identified based on the high degree of homology of their catalytic domain to that of the Ste20p from Saccharomyces cerevisiae.