Premium
Nerve growth factor stimulates tyrosine phosphorylation of paxillin in PC12h cells
Author(s) -
Khan Muhammad Ashraf,
Okumura Nobuaki,
Okada Masato,
Kobayashi Shin,
Nakagawa Hachiro
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00250-d
Subject(s) - paxillin , tyrosine phosphorylation , phosphorylation , ptk2 , tyrosine , microbiology and biotechnology , nerve growth factor , chemistry , signal transduction , protein tyrosine phosphatase , focal adhesion , biology , biochemistry , protein kinase c , receptor , mitogen activated protein kinase kinase
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.