SGER: Do NMDA and Non-NMDA Glutamate Receptors Share a Common Functional Domain?

谷氨酸受体是一种蛋白质，对脑细胞(神经元)之间的交流至关重要，并在包括学习和记忆在内的大脑过程中发挥作用。哺乳动物谷氨酸受体已进化为一个多基因家族，包含具有遗传、功能和药理相似性的亚型。谷氨酸受体在与细胞外谷氨酸(配体)结合时被激活。与受体的结合允许蛋白质打开一个通道(孔)，离子通过这个通道流过神经元膜；将化学信号(谷氨酸)转化为电信号(膜去极化)。这项拟议的研究将检验这样一个假设，即所有谷氨酸受体共有的一个区域(M3-M4胞外区)参与了一个共同的机制，即在配体结合部位和毛孔之间传递信号(变构信号转导)。阐明M3-M4胞外区的保守功能将为了解配体门控离子通道的功能提供重要的见解。

Glutamate receptors are proteins that are essential for communication between brain cells (neurons), and function in brain processes including learning and memory. Mammalian glutamate receptors have evolved into a multi-gene family containing subtypes with genetic, functional and pharmacological similarities. Glutamate receptors are activated when they bind extracellular glutamate (ligand). The binding to the receptor allows the protein to open a channel (pore) through which ions flow across the neuron's membrane; converting a chemical signal (glutamate) into an electrical signal (membrane depolarization). The proposed study will test the hypothesis that one region common to all glutamate receptors (the M3-M4 extracellular domain) participates in a common mechanism to relay the signal between the ligand binding site and the pore (allosteric signal transduction). Elucidation of a conserved functional role of the M3-M4 extracellular domain would provide important insights into how ligand-gated ion channels function.