FAF1

Official Full Name

Fas associated factor 1

Organism

Homo sapiens

GeneID

11124

Background

Interaction of Fas ligand (TNFSF6) with the FAS antigen (TNFRSF6) mediates programmed cell death, also called apoptosis, in a number of organ systems. The protein encoded by this gene binds to FAS antigen and can initiate apoptosis or enhance apoptosis initiated through FAS antigen. Initiation of apoptosis by the protein encoded by this gene requires a ubiquitin-like domain but not the FAS-binding domain. [provided by RefSeq, Jul 2008]

Synonyms

hFAF1; CGI-03; HFAF1s; UBXD12; UBXN3A;

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Detailed Information

FAF1 in oncogenesis

FAS-associated factor 1 (FAF1) is an evolutionarily conserved protein with many protein interaction domains. Even FAF1 was initially confirmed as one member of FAS death-inducing signaling complex, following work about it further demonstrated its functions in diverse biological processes. Convincing evidence supports that FAF1 involves in the regulation of apoptosis and NFκB activity as well as ubiquitination and proteasomal degradation, as a tumor suppressor, and highlights that FAF1's contribution to NFκB signaling transmission has critical connotations for human cancer treatment. Programmed cell death or apoptosis in a number of tissues is mediated by interactions among FAS and its corresponding ligands, which allow the occurrence of death-inducing signaling complex (DISC). FAF1 was recently characterized as effective regulator of cell survival, so how it works in the process of cancer or Parkinson's disease remains to be with more deeply elucidations. Disappearance or abnormity of FAF1 genes in human cancers suggests that it may be a tumor suppressor for its pro-apoptotic efficacy. There is still a long way to the full revelation of linkages between the FAF1 status and NFκB pathway in tumor, and answer the question of whether loss of FAF1 influences other signaling pathways in cancer due to its diversative protein interacting domains.

FAF1 regulates antiviral immunity through MAVS inhibition while antagonized by viral infection induced phosphorylation

An adaptor of innate immune receptor retinoic acid inducible gene1 (RIG-I), Mitochondrial antiviral signaling protein (MAVS), can connect the viral RNA recognition with antiviral signaling by accumulation of E3 ligase TRIM31 initiated lysine 63-linked poly-ubiquitination activating downstream signaling effectors. Aggregation of scaffold protein FAF1 gives a negative regulation to MAVS. Poly-ubiquitination and aggregation of MAVS were antagonized by FAF1 through its competition for the MAVS association with TRIM31. FAF1 knockout mice and FAF1 deficient myeloid cells are both shown with reduced viral load in vivo. Interaction with RIG-1 and lysine 63 poly-ubiquitination are vital for MAVS aggregation at the mitochondria, which acts as a critical step forward the initiation of antiviral responses. A recent date demonstrates repression of RNA virus induced MAVS-Lys63 poly-ubiquitination and aggregation and upcoming IFN-b birth and innate antiviral immunity by FAF1 is mitochondria relevant, moreover, mitochondria associated FAF1 come into aggregates together in cells associated with MAVS and without virus infection, while it is dismissed by IKKε-mediated-phosphorylation triggered acetylation and lysosomal degradation upon virus infection.

Fig 1. Signaling pathways intersections answer FAF1 role in Chondrogenesis (Miikka et al. 2011)

References:

Tong Dai, Liming Wu, Shuai Wang. (2018) 'FAF1 Regulates Antiviral Immunity by Inhibiting MAVS but Is Antagonized by Phosphorylation upon Viral Infection', Cell Host & Microbe, 2018, doi: 10.1016/j.chom.2018.10.006.
Craig W. Menges, Deborah A. Altomare & Joseph R. Testa. (2009) 'FAS-Associated Factor 1 (FAF1): Diverse functions and implications for oncogenesis', Cell Cycle, doi: 10.4161/cc.8.16.9280.
MichellaGhassibe-Sabbagh, LaurenceDesmyter, TobiasLangenberg. (2011) 'FAF1, a Gene that Is Disrupted in Cleft Palate and Has Conserved Function in Zebrafish'. AJHG, doi: 10.1016/j.ajhg.2011.01.003.

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