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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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Commentary

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

{ddagger} Author for correspondence (e-mail: crispy4{at}med.unc.edu)

Recent studies have demonstrated that mitogen-activated protein kinases (MAPKs), including Jun N-terminus kinase (JNK), p38 and Erk, play crucial roles in cell migration. JNK, for example, regulates cell migration by phosphorylating paxillin, DCX, Jun and microtubule-associated proteins. Studies of p38 show that this MAPK modulates migration by phosphorylating MAPK-activated protein kinase 2/3 (MAPKAP 2/3), which appears to be important for directionality of migration. Erk governs cell movement by phosphorylating myosin light chain kinase (MLCK), calpain or FAK. Thus, the different kinases in the MAPK family all seem able to regulate cell migration but by distinct mechanisms.

Key words: Cell migration, JNK, p38, Erk, Paxillin, Phosphorylation




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