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Caspase-10 is an initiator caspase in death receptor signaling.

A role for caspase-10, previously implicated in the autoimmune lymphoproliferative syndrome, in death receptor signaling has not been directly shown. Here we show that caspase-10 can function independently of caspase-8 in initiating Fas- and tumor necrosis factor-related apoptosis-inducing ligand-receptor-mediated apoptosis. Moreover, Fas crosslinking in primary human T cells leads to the recruitment and activation of caspase-10. Fluorescent resonance energy transfer analysis indicates that the death-effector domains of caspase-8 and -10 both interact with the death-effector domain of FADD. Nonetheless, we find that caspase-8 and -10 may have different apoptosis substrates and therefore potentially distinct roles in death receptor signaling or other cellular processes.

Pubmed ID: 11717445 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Antigens, CD95 | Apoptosis | Apoptosis Regulatory Proteins | B-Lymphocytes | Carrier Proteins | Caspase 10 | Caspase 8 | Caspase 9 | Caspases | Cells, Cultured | Dendritic Cells | Dimerization | Enzyme Activation | Fas-Associated Death Domain Protein | Gene Expression Profiling | Humans | Jurkat Cells | Membrane Glycoproteins | Signal Transduction | T-Lymphocytes | TNF-Related Apoptosis-Inducing Ligand | Tumor Necrosis Factor-alpha

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