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Published 29 October 2001. doi:10.1083/jcb.200106070
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© The Rockefeller University Press, 0021-9525/2001/10/459 $5.00
The Journal of Cell Biology, Volume 155, Number 3, October 29, 2001 459-470

Article

 Apoptosis of adherent cells by recruitment of caspase-8 to unligated integrins

Dwayne G. Stupack, Xose S. Puente, Souphaphone Boutsaboualoy, Chris M. Storgard and David A. Cheresh

Department of Immunology and Department of Vascular Biology, The Scripps Research Institute, La Jolla, CA 92037

Address correspondence to David Cheresh, The Scripps Research Institute, Department of Immunology, IMM24 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (858) 784-8281. Fax: (858) 784-8926. E-mail: cheresh{at}scripps.edu

Integrin-mediated adhesion promotes cell survival in vitro, whereas integrin antagonists induce apoptosis of adherent cells in vivo. Here, we demonstrate that cells adherent within a three-dimensional extracellular matrix undergo apoptosis due to expression of unligated integrins, the ß subunit cytoplasmic domain, or its membrane proximal sequence KLLITIHDRKEF. Integrin-mediated death requires initiator, but not stress, caspase activity and is distinct from anoikis, which is caused by the loss of adhesion per se. Surprisingly, unligated integrin or ß integrin tails recruit caspase-8 to the membrane, where it becomes activated in a death receptor–independent manner. Integrin ligation disrupts this integrin–caspase containing complex and increases survival, revealing an unexpected role for integrins in the regulation of apoptosis and tissue remodeling.

Key Words: cell adhesion; apoptosis; caspase; integrin; ligands


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