Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis.
Caspase-2 was reported to be involved in a number of apoptotic pathways triggered by various stimuli. However, the molecular mechanism of procaspase-2 activation in the course of apoptosis remains poorly defined. In this report, we demonstrate that procaspase-2 is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex (DISC) in human T- and B-cell lines. We show that procaspase-2 is activated at the DISC on CD95 stimulation. Despite its presence at the DISC, caspase-2 does not initiate apoptosis on CD95 stimulation in caspase-8-deficient cell lines. Taken together, our data reveal that caspase-2 is activated at the DISC but does not play an initiating role in the CD95-induced apoptosis.
Lavrik
Inna N
IN
Division of Immunogenetics, Tumorimmunology Program, German Cancer Research Center, Heidelberg. i.lavrik@dkfz.de
Golks
Alexander
A
Baumann
Simone
S
Krammer
Peter H
PH
D017209:Apoptosis; D001402:B-Lymphocytes; D053143:Caspase 2; D020169:Caspases / Q000378:metabolism* / Q000502:physiology; D045744:Cell Line, Tumor; D053418:Death Domain Receptor Signaling Adaptor Proteins; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D006801:Humans; D015398:Signal Transduction; D013601:T-Lymphocytes; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / Q000378:metabolism; D019014:fas Receptor / Q000378:metabolism* / Q000502:physiology
D053418:Death Domain Receptor Signaling Adaptor Proteins; D004792:Enzyme Precursors; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins; D019014:fas Receptor; D053143:Caspase 2; D020169:Caspases