MOLECULAR NEUROSCIENCEHigh-frequency synaptic stimulation induces association of fyn and c-src to distinct phosphorylated componentsLauri, S E.1,2; Taira, T1; Rauvala, H1Author Information 1Laboratory of Molecular Neurobiology, Institute of Biotechnology and Department of Biosciences, Division of Animal Physiology, P.O.Box 17, 00014 University of Helsinki, Finland 2Corresponding Author: S. E. Lauri Acknowledgements: We thank Kirsi Kenkkilä and Seija Lehto for technical assistance and the Sigrid Juselius Foundation and the Academy of Finland for financial support. Received 11 January 2000; accepted 21 January 2000 NeuroReport: April 7, 2000 - Volume 11 - Issue 5 - p 997-1000 Buy Abstract Signaling via tyrosine kinases appears necessary for regulation of synaptic efficacy. Interactions of the src-family kinases with phosphorylated proteins were studied in area CA1 of rat hippocampal slices 10 min after induction of long-term potentiation (LTP) by 100 Hz/1 s stimulation (HFS). HFS enhanced association of the src-family kinases fyn and c-src with an ∼120 kDa tyrosine phosphorylated component containing the focal adhesion kinase (FAK) and its homologue PYK2. Association of fyn with FAK and of c-src with PYK2 was increased following the HFS. Further, increase in tyrosine phosphorylation of PYK2 was detected following the HFS. These results suggest that fyn and c-src are involved in distinct signaling pathways and provide evidence for activation of FAK and PYK2 following synaptic stimulation inducing LTP in vitro. © 2000 Lippincott Williams & Wilkins, Inc.