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Perspectives
Emerging Roles for the Death Adaptor FADD in Death Receptor Avidity and Cell Cycle Regulation
Milton H. Werner, Chaowei Wu and Craig M. Walsh
volume 5 | issue 20
15 october 2006Pages: 2332 - 2338
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The Fas-associated death domain protein FADD is best known as an adaptor protein that senses a signal received at a death receptor and nucleates the assembly of the death-inducing signaling complex. Recent work reveals unexpected properties for this signaling protein, suggesting new roles for FADD in apoptotic signaling and in non-apoptotic functions linked to chemical modification of the FADD C-terminus. These new studies suggest novel types of high valency complexes may form in the plasma membrane and in the nucleus, raising intriguing questions as to how FADD senses the environment and responds to different signaling inputs to promote a biochemical response. In particular, we discuss the role of FADD in death receptor avidity and examine the relationship between FADD phosphorylation and subcellular localization with respect to various biological functions. Since FADD serves to modulate both apoptosis and cell cycle progression, these new findings promote the concept that differential complex assembly dictates disparate cellular processes mediated by this adaptor molecule.
Authors
Milton H. Werner
The Rockefeller University, New York, NY
Chaowei Wu
The Rockefeller University, New York, NY
Craig M. Walsh
University of California; Irvine, CA
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.