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MAP kinases and cell migration

Journal of Cell Science · 2004 · Vol. 117(20) · pp. 4619–4628
Cai HuangKen JacobsonMichael D. Schaller

Abstract

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.

Cellular Mechanics and InteractionsMelanoma and MAPK PathwaysProtein Kinase Regulation and GTPase SignalingCell biologyBiologyKinaseMAPK/ERK pathwayp38 mitogen-activated protein kinasesMyosin light-chain kinaseMitogen-activated protein kinaseCell migrationPhosphorylationPaxillin

MeSH terms

AnimalsCalpainCell MovementCytoskeletal ProteinsCytoskeletonMicrotubule-Associated ProteinsMitogen-Activated Protein KinasesMAP Kinase Signaling System

Funding

  • National Institutes of Health
Citations
1,049
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Cited by
MAP kinase signalling pathways in cancer
Oncogene · 2007 · 2,984 citations
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