JNK phosphorylation of paxillin, acting through the Rac1 and Cdc42 signaling cascade, mediates neurite extension in N1E-115 cells

被引:37
|
作者
Yamauchi, Junji [1 ]
Miyamoto, Yuki [1 ]
Sanbe, Atsushi [1 ]
Tanoue, Akito [1 ]
机构
[1] Natl Res Inst Child Hlth & Dev, Dept Pharmacol, Tokyo 1578535, Japan
关键词
paxillin; JNK; Rac1; Cdc42; Ser phosphorylation; neurite extension;
D O I
10.1016/j.yexcr.2006.05.016
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Neurons extend neurites from the cell body before formation of the polarized processes of an axon and dendrites. Neurite outgrowth involves remodeling of the cytoskeletal components, which are initially regulated by small GTPases of the Rho family. Here we show that c-Jun N-terminal kinase (JNK), which is controlled by Rho GTPases Rac1 and Cdc42, is activated following neurite extension in mouse N1E-115 neuroblastoma cells as a model. The extension is inhibited by JNK inhibitors (SP600125 and the small JNK-binding peptide) and Clostridium difficile Toxin B, the inhibitor for Rho GTPases. Additionally, paxillin, the multifunctional focal adhesion protein, is phosphorylated at Ser 178 by upregulation of the Rac1/Cdc42/JNK cascade. Conversely, transfection of the paxillin construct harboring the Ser 178-to-Ala mutation into cells inhibits neurite extension. Taken together, these results suggest the novel role of the Rac1/Cdc42/JNK signaling cascade in neurite extension and indicate that the downstream target paxillin may be one of the convergent points of various signaling pathways underlying neurite extension. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:2954 / 2961
页数:8
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