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These receptors have a cysteine-rich extracellular domain, which is a common feature of the TNFR superfamily, and a homologous cytoplasmic sequence termed the death domain (DD) (6).
The Fas DD consists of six amphipathic α-helices arranged antiparallel to one another, with side chains of hydrophobic residues forming an extensive network of interactions that constitute the core of the protein.
Fas (APO-1/CD95) is a cell surface receptor that initiates apoptotic pathways, and its cytoplasmic domain interacts with various molecules suggesting that Fas signaling is complex and regulated by multiple proteins. Here, we demonstrate that Ca M binds to Fas directly and identify the Ca M-binding site on the cytoplasmic death domain (DD) of Fas.
These findings suggest a novel function of Ca M in Fas-mediated apoptosis.
FADD also has a death effector domain that binds to an analogous domain in caspase-8 (9).
Several other cytoplasmic proteins that can bind to Fas have been identified, including Daxx (10), FAP-1 (Fas-associated phosphatase-1) (11), RIP (receptor-interacting protein) (12), and FAF1 (Fas-associated factor 1) (13).
Other death receptors, such as tumor necrosis factor receptor, DR4, and DR5 do not bind to Ca M.
The interaction between Fas and Ca M is Ca-dependent.