首页> 外文期刊>The Journal of Physiology >Intricate vascular architecture revealed after removing the scaffolding: PSD95 crucial for vascular Kv1 function.
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Intricate vascular architecture revealed after removing the scaffolding: PSD95 crucial for vascular Kv1 function.

机译:移除支架后揭示了复杂的血管结构:PSD95对血管Kv1功能至关重要。

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摘要

Post-synaptic density protein 95 (PSD95) is a key component of the complex signalling hierarchy in post-synaptic neuronal membranes. In neurones it is highly abundant and combines with an array of molecules including G-protein-coupled receptors, NO synthase, guanine nucleotide exchange factors, tyrosine kinases, anchoring proteins and motor proteins through separate PDZ, Src homology and guanylate kinase-like domains (Kim & Sheng, 2004). This role as a multi-factorial scaffold, integrating a myriad of signals, is fundamental for effective neuro-transmission and the synaptic plasticity inherent to memory and learning. In fact it could be said that this protein Cassanova, intimate and promiscuous, defines neuronal activity with its removal, leading to aberrant neuronal transmission.
机译:突触后密度蛋白95(PSD95)是突触后神经元膜中复杂信号传导层次的关键组成部分。在神经元中,它高度丰富并与一系列分子结合,包括G蛋白偶联受体,NO合酶,鸟嘌呤核苷酸交换因子,酪氨酸激酶,锚定蛋白和运动蛋白,通过单独的PDZ,Src同源性和鸟苷酸激酶样结构域( Kim&Sheng,2004年)。这种作用是整合多种信号的多因素支架,对于有效的神经传递以及记忆和学习固有的突触可塑性至关重要。实际上,可以说这种蛋白质Cassanova亲密且混杂,通过去除它来定义神经元活性,从而导致异常的神经元传递。

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