Program in Cellular Neuroscience, Neurodegeneration and Repair (CNNR), Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510, United States.
Curr Opin Neurobiol. 2012 Jun;22(3):488-95. doi: 10.1016/j.conb.2011.09.005. Epub 2011 Oct 10.
At excitatory synapses in the brain, glutamate released from nerve terminals binds to glutamate receptors to mediate signaling between neurons. Glutamate receptors expressed in heterologous cells show ion channel activity. Recently, native glutamate receptors were shown to contain auxiliary subunits that modulate the trafficking and/or channel properties. The AMPA receptor (AMPAR) can contain TARP and CNIHs as the auxiliary subunits, whereas kainate receptor (KAR) can contain the Neto auxiliary subunit. Each of these auxiliary subunits uniquely modulates the glutamate receptors, and determines properties of native glutamate receptors. A thorough elucidation of the properties of native glutamate receptor complexes is indispensable for the understanding of the molecular machinery that regulates glutamate receptors and excitatory synaptic transmission in the brain.
在大脑中的兴奋性突触中，从神经末梢释放的谷氨酸与谷氨酸受体结合，介导神经元之间的信号传递。在异源细胞中表达的谷氨酸受体具有离子通道活性。最近，研究表明天然谷氨酸受体含有辅助亚基，可调节转运和/或通道特性。AMPA 受体 (AMPAR) 可以包含 TARP 和 CNIHs 作为辅助亚基，而 kainate 受体 (KAR) 可以包含 Neto 辅助亚基。这些辅助亚基中的每一个都独特地调节谷氨酸受体，并决定天然谷氨酸受体的特性。对天然谷氨酸受体复合物特性的彻底阐明，对于理解调节大脑中谷氨酸受体和兴奋性突触传递的分子机制是必不可少的。
