MAPK signaling pathway

The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Classical mitogen-activated protein kinase (MAPK) pathway activation begins at the cell membrane where small GTPases and various protein kinases phosphorylate MAPKKKs. Subsequently, MAPKKKs directly phosphorylate and activate MAPKKs. Once phosphorylated, activated MAPKs phosphorylate numerous cytoplasmic substrates and ultimately modulate transcription factors that drive context-specific gene expression. As shown in the following picture, mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5 that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signaling. Presumably each MAPKKK confers responsiveness to distinct stimuli.


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