NMDA受体信号复合体中蛋白质的相互作用

Protein-protein interactions in NMDA receptor signaling complex

谷氨酸能兴奋性突触的突触后密集区(postsynaptic density,PSD)包含多种受体蛋白、骨架蛋白和信号蛋白,它们通过分子中特定的结构域相互识别并动态地结合,形成多个信号复合体,参与突触后受体功能的调节及其下游特异性信号转导通路的激活。其中,NMDA受体信号复合体中蛋白质-蛋白质的相互作用及其调控机制的阐明,对于深入了解神经发育、突触可塑性、兴奋性毒性等生理病理的分子机制有重要意义。

Within the glutamatergic excitatory postsynaptic density (PSD), glutamate receptor subunits, scaffolding proteins and an array of signal transduction molecules are assembled into large multi-protein signaling complexes via the dynamic interactions between specific protein domains, which is responsible for the modulation of the NMDA receptor functions and activation of the downstream specific signaling cascades. Elucidating the roles and regulation mechamisms of the dynamic protein-protein interactions in NMDA receptor signaling complex serves critical functions in further understanding the molecular mechanisms of multiple physiological and pathological events including neuronal development, synaptic plasticity, learning, memory and diverse neurological disorders resulting from excitotoxicity.