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The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A.

The ectodermal dysplasia receptor (EDAR) is a recently isolated member of the tumor necrosis factor receptor family that has been shown to play a key role in the process of ectodermal differentiation. We present evidence that EDAR is capable of activating the nuclear factor-kappaB, JNK, and caspase-independent cell death pathways and that these activities are impaired in mutants lacking its death domain or those associated with anhidrotic ectodermal dysplasia and the downless phenotype. Although EDAR possesses a death domain, it did not interact with the death domain-containing adaptor proteins TRADD and FADD. EDAR successfully interacted with various TRAF family members; however, a dominant-negative mutant of TRAF2 was incapable of blocking EDAR-induced nuclear factor-kappaB or JNK activation. Collectively, the above results suggest that EDAR utilizes a novel signal transduction pathway. Finally, ectodysplasin A can physically interact with the extracellular domain of EDAR and thus represents its biological ligand.

Pubmed ID: 11035039

Authors

  • Kumar A
  • Eby MT
  • Sinha S
  • Jasmin A
  • Chaudhary PM

Journal

The Journal of biological chemistry

Publication Data

January 26, 2001

Associated Grants

  • Agency: NIAMS NIH HHS, Id: P30 AR41940-09

Mesh Terms

  • Cell Death
  • Ectodermal Dysplasia
  • Ectodysplasins
  • Enzyme Activation
  • JNK Mitogen-Activated Protein Kinases
  • Membrane Proteins
  • Mitogen-Activated Protein Kinases
  • Mutagenesis
  • NF-kappa B
  • Protein Binding
  • Protein-Serine-Threonine Kinases
  • Receptors, Tumor Necrosis Factor
  • Signal Transduction