丝裂原活化蛋白激酶与细胞迁移。

MAP kinases and cell migration.

作者信息

Huang Cai, Jacobson Ken, Schaller Michael D

机构信息

Department of Cell and Developmental Biology, University of North Carolina, Chapel Hill, NC 27599-7090, USA.

出版信息

J Cell Sci. 2004 Sep 15;117(Pt 20):4619-28. doi: 10.1242/jcs.01481.

DOI:10.1242/jcs.01481

PMID:15371522

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.

摘要

最近的研究表明，丝裂原活化蛋白激酶（MAPK），包括Jun氨基末端激酶（JNK）、p38和细胞外信号调节激酶（Erk），在细胞迁移中起关键作用。例如，JNK通过磷酸化桩蛋白、双皮质素（DCX）、Jun和微管相关蛋白来调节细胞迁移。对p38的研究表明，这种MAPK通过磷酸化丝裂原活化蛋白激酶激活的蛋白激酶2/3（MAPKAP 2/3）来调节迁移，这似乎对迁移的方向性很重要。Erk通过磷酸化肌球蛋白轻链激酶（MLCK）、钙蛋白酶或粘着斑激酶（FAK）来控制细胞运动。因此，MAPK家族中的不同激酶似乎都能够调节细胞迁移，但机制不同。