Fas-associated protein 1 (FAF1) was initially identified as a Fas-binding pro-apoptotic protein that is component of the death-inducing signaling complex in Fas-mediated apoptosis (1). FAF1 can also induce apoptosis in the absence of extrinsic death signals when overexpressed although it does not contain typical death motifs such as the death domain, death effector domain, and caspase recruitment domain (1,2). Overexpression of FAF1 also decreases the basal level of NF-kappaB activity in transfected 293 cells, inhibits NF-kappaB activity induced by TNF-alpha, IL-1beta and lipopolysaccharide, and prevents NF-kappaB translocation to the nucleus (3), suggesting that another role of FAF1 is to negatively regulate the activity of NF-kappaB. FAF1 can also interact with the inflammatory signaling PYRIN-containing Apaf-1-like proteins (PYPAFs, also called NALPs) such as PYPAF1, PYPAF2 (NALP2), and PYPAF7, suggesting FAF1 may also be involved in the inflammation pathway (4). Multiple differentially spliced isoforms of FAF1 are known to exist.
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