NERVE GROWTH-FACTOR STIMULATES TYROSINE PHOSPHORYLATION OF PAXILLIN IN PC12H CELLS

被引：21

作者：

KHAN, MA

OKUMURA, N

OKADA, M

KOBAYASHI, S

NAKAGAWA, H

机构：

[1] Division of Protein Metabolism, Institute for Protein Research, Osaka University, Suita, Osaka

来源：

FEBS LETTERS | 1995年 / 362卷 / 02期

关键词：

NERVE GROWTH FACTOR; PC12; PAXILLIN; NEURONAL DIFFERENTIATION;

D O I：

10.1016/0014-5793(95)00250-D

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nerve growth factor (NGF) induces tyrosine phosphorylation of various cellular proteins to activate multiple signal transduction pathways, We show that one of these proteins is paxillin, a cytoskeletal component associated with adhesion plaques, Phospho-amino acid analysis showed that NGF stimulated phosphorylation of its serine in addition to tyrosine residues, Tyrosine phosphorylation of paxillin by NGF was blocked by the pretreatment of the cells with cytochalasin D, an inhibitor of actin polymerization. These results suggest that phosphorylation of paxillin is involved in the signaling pathway of NGF in PC12 cells.

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页码：201 / 204

页数：4

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