Caspase 3 Cleavage of the Ste20-Related Kinase SLK Releases and Activates an Apoptosis-Inducing Kinase Domain and an Actin-Disassembling Region

• DOI: 10.1128/mcb.20.2.684-696.2000
• Publication Date: 2002-07-27T10:06:23Z
• Authors: Luc A. Sabourin; Patrick Seale; Julian Wagner; Michael A. Rudnicki
• Keywords: Stress fiber; ASK1

We have demonstrated that a novel Ste20-related kinase, designated SLK, mediates apoptosis and actin stress fiber dissolution through distinct domains generated by caspase 3 cleavage. Overexpression of SLK in C2C12 myoblasts stimulated the disassembly fibers focal adhesions induced apoptosis, as determined annexin V binding terminal deoxynucleotidyltransferase-mediated dUTP-biotin nick end labeling analysis. was cleaved vitro vivo during c-Myc-, tumor necrosis factor alpha, UV-induced apoptosis. Furthermore, cleavage released two with activities: an activated N-terminal kinase domain promoted cytoskeletal rearrangements C-terminus disassembled fibers. Moreover, our analysis has identified conserved region (termed AT1-46 homology domain) efficiently promotes disassembly. Finally, transient transfection also c-Jun signaling pathway. Our results suggest caspase-activated represents effector remodeling