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Local substrates of non-receptor tyrosine kinases at synaptic sites in neurons

Li-Min Mao¹, Ryan Geosling², Brian Penman², John Q. Wang^1,2,*

¹Department of Basic Medical Science, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA；²Department of Anesthesiology, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA

Abstract

Several non-receptor tyrosine kinase (nRTK) members are expressed in neurons of mammalian brains. Among these neuron- enriched nRTKs, two Src family kinase members (Src and Fyn) are particularly abundant at synaptic sites and have been most extensively studied for their roles in the regulation of synaptic activity and plasticity. Increasing evidence shows that the synaptic subpool of nRTKs interacts with a number of local substrates, including glutamate receptors (both ionotropic and metabotropic glutamate receptors), postsynaptic scaffold proteins, presynaptic proteins, and synapse-enriched enzymes. By phosphorylating specific tyrosine residues in the intracellular domains of these synaptic proteins either constitutively or in an activity-dependent manner, nRTKs regulate these substrates in trafficking, surface expression, and function. Given the high sensitivity of nRTKs to changing synaptic input, nRTKs are considered to act as a critical regulator in the determination of the strength and efficacy of synaptic transmission.

Key words: N-methyl-D-aspartic acid; α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid ; metabotropic glutamate receptor ; postsynaptic density protein 95 ; Src ; Fyn ; ERK ; Cdk5 ; synaptophysin ; synapsin I

Received: 2017-03-17　　Accepted: 2017-09-12

Corresponding author: 王强　　E-mail: wangjq@umkc.edu

DOI: 10.13294/j.aps.2017.0067

Citing This Article：

Li-Min Mao, Ryan Geosling, Brian Penman, John Q. Wang. Local substrates of non-receptor tyrosine kinases at synaptic sites in neurons. Acta Physiol Sin 2017; 69 (5): 657-665