Protein kinase C and F-actin are essential for stimulation of neuronal FAK tyrosine phosphorylation by G-proteins and amyloid beta protein

摘要: Focal adhesion kinase (FAK) is a protein tyrosine implicated in signal transduction pathways for integrins, neuropeptides, and lysophosphatidic acid. FAK, first discovered non-neuronal cells, recently has been reported to occur neurons, where its phosphorylation upregulated by fibronectin the Alzheimer's Aβ peptide. The current work elucidated molecular events leading of FAK rat B103 CNS nerve cell line. Activation receptor-coupled G-proteins Mas-7 was found evoke rapid upregulation (Tyr(P)). Upregulation blocked GF109203X, potent inhibitor C (PKC). Phorbol ester also FAK-YP, verifying role PKC cascade. FAK-YP activation dependent upon intact F-actin, as cytochalasin D abolished stimulation phorbol ester. relatively slow increase evoked chronic exposure GF109203X D. results show that neurons regulated positively PKC, functioning down-stream from through an F-actin-dependent mechanism. peptide capable activating elements this same pathway, via membrane remain be determined.