Graduate Students

		Irene Ch'en Programmed cell death or apoptosis is essential for maintaining homeostasis within the immune system. Death receptor ligation leads to the recruitment of an adaptor molecule, Fas-associated death domain protein (FADD), to form the death inducing signaling complex (DISC). Caspase-8, a cysteine protease, is recruited to the death effector domain (DED) of this complex, initiating a proteolytic activation cascade of downstream effector Caspases-3 and -7 that results in apoptosis. However, this pathway mediated by death receptor signaling is still poorly characterized. Our lab has previously shown that FADD is required for the survival of peripheral T cells undergoing antigen driven proliferation in vitro. The loss of FADD also results in the failure to mount an antigen-specific response to an LCMV infection. To study the role of Caspase-8 in lymphocytes, we have generated mice with a conditional deletion of Caspase-8 and bred them to various Cre-recombinases. I am currently investigating its role in activation and survival.
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