FADD and its phosphorylation

IUBMB Life. 2004 Jul;56(7):395-401. doi: 10.1080/15216540400008929.


The adaptor protein FADD is essential for apoptosis induced by 'death receptors', mediating aggregation and autocatalytic activation of caspase-8. Surprisingly, FADD is also involved in regulating T and B cell development. Accumulating evidences now suggest that FADD and its phosphorylation have additional roles in controlling pathways of cellular activation and proliferation, while the kinase modifying FADD phosphorylation is still unidentified. The cellular localization of FADD may also contribute to define FADD's role in apoptosis or proliferation. FADD may be a pivotal molecule which coupling the opposite cell processes of proliferation and apoptosis. FADD, probably modulated by phosphorylation, may function as a 'cell renewal set point' co-regulating proliferation and apoptosis in parallel.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Adaptor Proteins, Signal Transducing / physiology*
  • Amino Acid Sequence
  • Animals
  • Apoptosis / physiology*
  • Caspase 8
  • Caspases / metabolism
  • Cell Proliferation*
  • Fas-Associated Death Domain Protein
  • Humans
  • Lymphocytes / physiology
  • Models, Biological
  • Molecular Sequence Data
  • Phosphorylation
  • Sequence Alignment
  • Signal Transduction / physiology*


  • Adaptor Proteins, Signal Transducing
  • FADD protein, human
  • Fas-Associated Death Domain Protein
  • CASP8 protein, human
  • Caspase 8
  • Caspases