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Eder Moscoso. Exons encode the intracellular region. Fas forms the death-inducing signaling complex DISC upon ligand binding.
Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes oligomerization of Fas. Recent studies which suggested the trimerization of Fas could not be validated.
To this end, several clever ways of trimerizing the antibody for in vitro research have been employed. Upon ensuing death domain DD aggregation, the receptor complex is internalized via the cellular endosomal machinery.
FLICE can then self-activate through proteolytic cleavage into p10 and p18 subunits, two each of which form the active heterotetramer enzyme.
Active caspase-8 is then released from the DISC into the cytosol, where it cleaves other effector caspases, eventually leading to DNA degradation, membrane blebbing, and other hallmarks of apoptosis.
Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant.
Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas.
This is stimulated by cancer-produced Fas ligand for optimal growth. Although Fas has been shown to promote tumor growth in the above mouse models, analysis of the human cancer genomics database revealed that FAS is not significantly focally amplified across a dataset of tumors FAS is not an oncogene , but is significantly focally deleted across the entire dataset of these tumors, [15] suggesting that FAS functions as a tumor suppressor in humans.
In cultured cells, FasL induces various types of cancer cell apoptosis through the Fas receptor. Some reports have suggested that the extrinsic Fas pathway is sufficient to induce complete apoptosis in certain cell types through DISC assembly and subsequent caspase-8 activation.
These cells are dubbed Type 1 cells and are characterized by the inability of anti-apoptotic members of the Bcl-2 family namely Bcl-2 and Bcl-xL to protect from Fas-mediated apoptosis.
However, evidence for crosstalk between the extrinsic and intrinsic pathways exists in the Fas signal cascade.
In most cell types, caspase-8 catalyzes the cleavage of the pro-apoptotic BH3-only protein Bid into its truncated form, tBid. Fas receptor has been shown to interact with:.
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