• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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


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


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