SLK Antibody #41255

SLK (Ste20-like Kinase) is a member of the germinal center kinase (GCK) family of proteins. SLK has a kinase domain located at the N terminus (1). The autophosphorylation of SLK at Thr183 and Ser189 is required for the upregulation of SLK kinase activity (1, 2). The protein also has a caspase cleavage site DXXD and a SH3 binding site PXXP located in the middle part of its sequence, and a regulatory C terminal coiled-coil domain for homodimerization and adaptor binding (1-4). SLK plays important roles in development, tissue regeneration and cancer cell migration by regulating several signaling pathways (5-7). SLK phosphorylates and activates ASK1 to induce downstream p38 phosphorylation and apoptosis (8,9). During cell cycle, SLK phosphorylates Polo-like kinase (PLK) at Thr210 to promote G2/M transition (10,11). SLK also promotes cell division by direct phosphorylation of ERMs and dynactin to activate microtubule reorganization and spindle orientation (12, 13). During focal adhesion and cell migration process, SLK is activated and colocalized to the focal adhesion complex where it promotes complex turnover by phosphorylating paxillin at Ser250 (14, 15).