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The CD95(APO-1/Fas) DISC and beyond.

M E Peter1, P H Krammer

  • 1The Ben May Institute for Cancer Research, University of Chicago, IL 60637, USA. mpeter@uchicago.edu

Cell Death and Differentiation
|March 26, 2003
PubMed
Summary
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CD95, a key death receptor, initiates apoptosis through its death domain, forming a death-inducing signaling complex (DISC). Recent research highlights proteins regulating DISC formation and activity in apoptosis.

Area of Science:

  • Cellular biology
  • Molecular biology
  • Immunology

Background:

  • CD95 (APO-1/Fas) is a critical death receptor involved in programmed cell death.
  • Its cytoplasmic tail contains an 80 amino acid death domain essential for signaling.
  • Activation by anti-CD95 antibodies or CD95 ligand triggers apoptosis.

Purpose of the Study:

  • To review recent advancements in understanding CD95-mediated apoptosis.
  • To highlight the role of the death-inducing signaling complex (DISC) in CD95 signaling.
  • To discuss regulatory proteins involved in DISC formation and activity.

Main Methods:

  • Literature review of recent studies on CD95 signaling.
  • Analysis of molecular mechanisms governing DISC assembly.

Related Experiment Videos

  • Examination of regulatory factors influencing apoptosis induction.

    • Main Results:

    • The death domain of CD95 is crucial for recruiting signaling molecules.
    • Formation of the DISC, comprising adaptor proteins and initiator caspases, is vital for apoptosis.
    • Several proteins have been identified that modulate DISC formation and function.

    Conclusions:

    • CD95-mediated apoptosis is a tightly regulated process.
    • Understanding DISC regulation provides insights into controlling programmed cell death.
    • Further research into regulatory proteins can reveal therapeutic targets for diseases involving apoptosis.