Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Blotting, Western
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Cell Adhesion Molecules / metabolism*
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Cytochalasin D / pharmacology
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Cytoskeletal Proteins / metabolism*
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Immunosorbent Techniques
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Kinetics
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Nerve Growth Factors / pharmacology*
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PC12 Cells / metabolism*
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Paxillin
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Phosphoproteins / metabolism*
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Phosphorylation
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Phosphoserine / metabolism
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Phosphotyrosine
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Rats
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Signal Transduction
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Tyrosine / analogs & derivatives*
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Tyrosine / metabolism
Substances
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Cell Adhesion Molecules
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Cytoskeletal Proteins
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Nerve Growth Factors
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Paxillin
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Phosphoproteins
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Pxn protein, rat
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Phosphoserine
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Phosphotyrosine
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Cytochalasin D
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Tyrosine