高频突触刺激诱导fyn和c-src与不同的磷酸化成分结合。

High-frequency synaptic stimulation induces association of fyn and c-src to distinct phosphorylated components.

作者信息

Lauri S E, Taira T, Rauvala H

机构信息

Laboratory of Molecular Neurobiology, University of Helsinki, Finland.

出版信息

Neuroreport. 2000 Apr 7;11(5):997-1000. doi: 10.1097/00001756-200004070-00020.

DOI:10.1097/00001756-200004070-00020

PMID:10790871

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 CAI of rat hippocampal slices 10 min after induction of long-term potentiation (LTP) by 100 Hz/l s stimulation (HFS). HFS enhanced association of the src-family kinases fyn and c-src with an approximately 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.

摘要

通过酪氨酸激酶进行信号传导似乎是调节突触效能所必需的。在通过100Hz/1s高频刺激（HFS）诱导长期增强（LTP）10分钟后，研究了src家族激酶与磷酸化蛋白在大鼠海马切片CA1区的相互作用。HFS增强了src家族激酶fyn和c-src与一个约120kDa的酪氨酸磷酸化成分的结合，该成分包含粘着斑激酶（FAK）及其同源物PYK2。HFS后，fyn与FAK以及c-src与PYK2的结合增加。此外，HFS后检测到PYK2的酪氨酸磷酸化增加。这些结果表明，fyn和c-src参与不同的信号通路，并为体外突触刺激诱导LTP后FAK和PYK2的激活提供了证据。