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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


  • Wang J
  • Chun HJ
  • Wong W
  • Spencer DM
  • Lenardo MJ


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

November 20, 2001

Associated Grants


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