c-FOS activation by phospho ERK1/2

Stable Identifier
R-HSA-450325
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
12134156 Molecular interpretation of ERK signal duration by immediate early gene products

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

Nat Cell Biol 2002
7588633 The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells

Okazaki, K, Sagata, N

EMBO J 1995
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein serine/threonine kinase activity of p-T,Y MAPK dimers [nucleoplasm]
Physical Entity
Activity
Orthologous Events
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Created