Cytoskeletal and phosphoinositide requirements for muscarinic receptor signaling to focal adhesion kinase and paxillin

Autor: Scott D. Sorensen, Daniel A. Linseman, Stephen K. Fisher, Edward L. McEwen
Rok vydání: 1998
Předmět:
Phosphatidylinositols
environment and public health
Biochemistry
Second Messenger Systems
Wortmannin
chemistry.chemical_compound
Neuroblastoma
Phosphatidylinositol Phosphates
Tumor Cells
Cultured
Tyrosine
Enzyme Inhibitors
Phosphorylation
Cytoskeleton
Protein-Tyrosine Kinases
Receptors
Muscarinic
Cell biology
biological phenomena
cell phenomena
and immunity
Cytochalasin D
Morpholines
PTK2
macromolecular substances
Biology
Muscarinic Agonists
Focal adhesion
Cellular and Molecular Neuroscience
GTP-Binding Proteins
Cell Adhesion
Humans
Lovastatin
Paxillin
Nucleic Acid Synthesis Inhibitors
Tyrosine phosphorylation
Actin cytoskeleton
Phosphoproteins
Actins
Receptor
Insulin
Androstadienes
enzymes and coenzymes (carbohydrates)
Cytoskeletal Proteins
chemistry
Chromones
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
biology.protein
Cell Adhesion Molecules
Phosphorus Radioisotopes
Zdroj: Journal of neurochemistry. 70(3)
ISSN: 0022-3042
Popis: The mechanism whereby agonist occupancy of muscarinic cholinergic receptors elicits an increased tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin has been examined. Addition of oxotremorine-M to SH-SY5Y neuroblastoma cells resulted in rapid increases in the phosphorylation of FAK (t(1/2) = 2 min) and paxillin that were independent of integrin-extracellular matrix interactions, cell attachment, and the production of phosphoinositide-derived second messengers. In contrast, the increased tyrosine phosphorylations of FAK and paxillin were inhibited by inclusion of either cytochalasin D or mevastatin, agents that disrupt the cytoskeleton. Furthermore, phosphorylation of FAK and paxillin could be prevented by addition of either wortmannin or LY-294002, under conditions in which the synthesis of phosphatidylinositol 4-phosphate was markedly attenuated. These results indicate that muscarinic receptor-mediated increases in the tyrosine phosphorylation of FAK and paxillin in SH-SY5Y neuroblastoma cells depend on both the maintenance of an actin cytoskeleton and the ability of these cells to synthesize phosphoinositides.
Databáze: OpenAIRE
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