Function
Mitogen-activated protein kinase (MAPK) also known as Extracellular Signal-Regulated Kinase (ERK) are serine/threonine kinases which regulate various cellular activities in response to extracellular stimuli by mitogens, heat shock and more. MAPK is part of the MAPK cascade which consists of MAPK, MAP2K and MAP3K which are activated by phosphorylation[1].
- MAPK1 and MAPK3 are activated in response to growth factors.
- For MAPK2 representations see Michael Roberts/BIOL115/ERK2.
- MAPK6 is activated by phorbol esters.
- MAPK7 is activated by stress stimuli.
- MAPK8 (called also c-Jun N-terminal kinase 1 or JNK1), MAPK9, MAPK10 (called also c-Jun N-terminal kinase 3 or JNK3), MAPK11, MAPK12, MAPK13, MAPK14 are stress-activated.
- MAPK11 (also called p38-β MAPK), MAPK12 (also called p38-γ MAPK), MAPK13 (also called p38-δ MAPK), MAPK14 (also called p38-α MAPK) belongs to the class called p38 MAPK.
Relevance
MAPK cascade is elevated in cancer cells, hence MAPK inhibitors are tested as potential cancer therapy.
Disease
MAPK14 is associated with acquired hyperkeratosis and prostate transitional cell carcinoma.
3D Structures of Mitogen-activated protein kinase
Updated on 28-April-2016
References
- ↑ Robinson MJ, Cobb MH. Mitogen-activated protein kinase pathways. Curr Opin Cell Biol. 1997 Apr;9(2):180-6. PMID:9069255
