FOS
The Fos gene family consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. These genes encode leucine zipper proteins that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. As such, the FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation. In some cases, expression of the FOS gene has also been associated with apoptotic cell death.
Full Name
Fos Proto-Oncogene, AP-1 Transcription Factor Subunit
Alternative Names
Fos Proto-Oncogene, AP-1 Transcription Factor Subunit; FBJ Murine Osteosarcoma Viral Oncogene Homolog; G0/G1 Switch Regulatory Protein 7; FBJ Murine Osteosarcoma Viral (V-Fos) Oncogene Homolog (Oncogene FOS); V-Fos FBJ Murine Osteosarcoma Viral Oncogene Homolog; Fos Proto-Oncogene, AP-1 Trancription Factor Subunit; Cellular Oncogene C-Fos; Cellular Oncogene Fos;
Function
Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.
Biological Process
Aging Source: Ensembl
Cellular response to cadmium ion Source: CAFA
Cellular response to calcium ion Source: Ensembl
Cellular response to extracellular stimulus Source: Ensembl
Cellular response to hormone stimulus Source: Ensembl
Cellular response to reactive oxygen species Source: BHF-UCL
Conditioned taste aversion Source: Ensembl
DNA methylation Source: ProtInc
Female pregnancy Source: Ensembl
Inflammatory response Source: ProtInc
Nervous system development Source: Ensembl
Positive regulation of neuron death Source: ARUK-UCL
Positive regulation of osteoclast differentiation Source: Ensembl
Positive regulation of pri-miRNA transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: CAFA
Regulation of transcription by RNA polymerase II Source: GO_Central
Response to cAMP Source: Ensembl
Response to cold Source: Ensembl
Response to corticosterone Source: Ensembl
Response to cytokine Source: Ensembl
Response to drug Source: Ensembl
Response to gravity Source: Ensembl
Response to immobilization stress Source: Ensembl
Response to light stimulus Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Response to muscle stretch Source: Ensembl
Response to progesterone Source: Ensembl
Response to toxic substance Source: Ensembl
Skeletal muscle cell differentiation Source: Ensembl
Sleep Source: Ensembl
SMAD protein signal transduction Source: BHF-UCL
Transcription by RNA polymerase II Source: ProtInc
Transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Cellular Location
Cytosol; Endoplasmic reticulum; Nucleus. In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30.
PTM
Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity).
Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232.
In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis.
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