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Caspase-8 Promotes Cell Motility and Calpain Activity under Nonapoptotic Conditions

¹ Mary Babb Randolph Cancer Center and Department of Biochemistry, West Virginia University, Morgantown, West Virginia; ² The Burnham Institute, La Jolla, California; ³ Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel; and ⁴ Department of Genetics and Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee

Requests for reprints: Steven M. Frisch, Mary Babb Randolph Cancer Center and Department of Biochemistry, West Virginia University, 1 Medical Center Drive, POB 9300, Morgantown, WV 26506. Phone: 304-293-2980; E-mail: sfrisch{at}hsc.wvu.edu.

Significant caspase-8 activity has been found in normal and certain tumor cells, suggesting that caspase-8 possesses an alternative, nonapoptotic function that may contribute to tumor progression. In this article, we report that caspase-8 promotes cell motility. In particular, caspase-8 is required for the optimal activation of calpains, Rac, and lamellipodial assembly. This represents a novel nonapoptotic function of caspase-8 acting at the intersection of the caspase-8 and calpain proteolytic pathways to coordinate cell death versus cell motility signaling. (Cancer Res 2006; 66(8): 4273-8)

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