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First published online September 15, 2004
doi: 10.1242/10.1242/jcs.01481

Journal of Cell Science 117, 4619-4628 (2004)
Published by The Company of Biologists 2004
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MAP kinases and cell migration

Cai Huang1,*, Ken Jacobson1,2,3 and Michael D. Schaller1,2,3,{ddagger}

1 Department of Cell and Developmental Biology, University of North Carolina, Chapel Hill, NC 27599-7090, USA
2 Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599-7090, USA
3 Comprehensive Center for Inflammatory Disorders, University of North Carolina, Chapel Hill, NC 27599-7090, USA



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  		Fig. 1. Signaling pathways for cell migration mediated by JNK. Extracellular stimuli, such as serum, EGF and TGF-ß, activate MEKK1 through FAK/Src or Rac. Active MEKK1 phosphorylates and activates MKK4 or MKK7, which then phosphorylates and activates JNK. The activated JNK in turn phosphorylates Jun, paxillin, Spir, DCX and MAPs. Paxillin phosphorylation might facilitate cell adhesion turnover, thus promoting rapid migration of cells. The phosphorylation of DCX, MAP1B and MAP2 might promote microtubule dynamics, thus enhancing neuronal migration. The phosphorylation of Jun is also involved in cell migration, but the mechanism is unknown. Spir phosphorylation might also play a role in actin dynamics and cell migration. MT, microtubule. Orange lines represent speculative pathways.

 


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  		Fig. 2. Signaling pathways for cell migration mediated by p38. Chemotactic factors and growth factors, such as fMLP, VEGF and FGF, activate MKK3/6 via their upstream MAPKKKs, such as MLK3. Activated MKK3/6 phosphorylate and activate p38, which in turn activates MAPKAPK2/3. The active MAPKAPK2/3 then phosphorylate HSP-27, resulting actin reorganization and cell migration. MAPKAPK2/3 also phosphorylates the p16-Arc of the Arp2/3 complex and 5-lipoxygenase, whereas p38 phosphorylates paxillin and caldesmon. These might play roles in cell migration. Orange lines represent speculative pathways.

 


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  		Fig. 3. Signaling pathways for cell migration mediated by Erk. Growth factors, such as PDGF, EGF and FGF, activate Erk through the Ras-Raf-MEK1/2-Erk signaling module. Activated Erk regulates membrane protrusions and focal adhesion turnover via phosphorylating MLCK and promotes focal adhesion disassembly via phosphorylating and activating calpain. Phosphorylation of FAK and paxillin by Erk may regulate focal adhesion dynamics, probably by influencing the paxillin-FAK interaction. Orange lines represent speculative pathways.

 




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