A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain

We describe the cloning of a protein that binds to the death domain of Fas/APOI and is apparently involved in the cytotoxic triggering process

Mark P. Boldin; Eugene E. Varfolomeev; Zeev Pancer; Igor L. Mett; Jacques H. Camonis; David Wallach

2002

Scholarcy highlights

  • From the Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, Israel 76100 and ┬žDenis Diderot University, Inserm Unit 248, Paris 75010, France
  • Signaling for cell death by Fas/APOI occurs via a distinct region in its intracellular domain
  • The tumor necrosis factorl receptors and the structurally related receptor Fas/APOI trigger destructive activities in cells upon stimulation by leukocyte-produced ligands that lead to their own demise
  • We describe the cloning of a protein that binds to the death domain of Fas/APOI and is apparently involved in the cytotoxic triggering process
  • Thi s se lf-binding and th e binding of MORTI to Fa s/APOI involve differen t regions of th e protein
  • A fragment corresponding to residues 130-245 bind s to Fa s/APOI but does not bind to MORTI
  • Thi s part of th e death domain shows simila rity to a region in the intracellular domain of t he low a ffinity nerve growth factor receptor 23, a receptor whose extracellular domain is know n to contain a not her conse rved seq ue nce motif common to Fas/APO I, the TN F receptors, an d ot her mem bers of the tumor necrosis factor/N GF receptor fa mily

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