c-FOS activation by phospho ERK1/2

Stable Identifier
Reaction [transition]
Homo sapiens
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The Fos proteins(c-Fos, FosB, Fra1 and Fra2), which cannot homodimerize, form stable heterodimers with Jun proteins and thereby enhance their DNA binding activity.

On activation of the MAPK pathway, Ser-374 of Fos is phosphorylated by ERK1/2 and Ser-362 is phosphorylated by RSK1/2, the latter kinases being activated by ERK1/2. If stimulation of the MAPK pathway is sufficiently sustained, ERK1/2 can dock on an upstream FTYP amino acid motif, called the DEF domain (docking site for ERKs, FXFP), and phosphorylate Thr-331 and Thr-325.

Phosphorylation at specific sites enhances the transactivating potential of several AP-1 proteins, including Jun and Fos, without having any effect on their DNA binding activities. Thus, phosphorylation of Ser-362 and Ser-374 stabilizes c-Fos but has no demonstrated role in the control of transcriptional activity. On the contrary, phosphorylation of Thr-325 and Thr-331 enhances c-Fos transcriptional activity but has no demonstrated effect on protein turnover.

Literature References
PubMed ID Title Journal Year
7588633 The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells

Sagata, N, Okazaki, K

EMBO J 1995
12134156 Molecular interpretation of ERK signal duration by immediate early gene products

Murphy, LO, Blenis, J, Chen, RH, Fingar, DC, Smith, S

Nat Cell Biol 2002
Catalyst Activity

protein serine/threonine kinase activity of p-T,Y MAPK dimers [nucleoplasm]

Orthologous Events
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