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钙调蛋白和 CaMKII 在缝隙连接蛋白 36 可塑性中的作用。

The Roles of Calmodulin and CaMKII in Cx36 Plasticity.

机构信息

Department of Biology & Center for Vision Research (CVR), York University, Toronto, ON M3J 1P3, Canada.

Dominick P. Purpura Department of Neuroscience & Department of Medicine (Cardiology), Albert Einstein College of Medicine, New York, NY 10461, USA.

出版信息

Int J Mol Sci. 2021 Apr 25;22(9):4473. doi: 10.3390/ijms22094473.

DOI:10.3390/ijms22094473
PMID:33922931
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8123330/
Abstract

Anatomical and electrophysiological evidence that gap junctions and electrical coupling occur between neurons was initially confined to invertebrates and nonmammals and was thought to be a primitive form of synaptic transmission. More recent studies revealed that electrical communication is common in the mammalian central nervous system (CNS), often coexisting with chemical synaptic transmission. The subsequent progress indicated that electrical synapses formed by the gap junction protein connexin-36 () and its paralogs in nonmammals constitute vital elements in mammalian and fish synaptic circuitry. They govern the collective activity of ensembles of coupled neurons, and gap junctions endow them with enormous adaptive plasticity, like that seen at chemical synapses. Moreover, they orchestrate the synchronized neuronal network activity and rhythmic oscillations that underlie the fundamental integrative processes, such as memory and learning. Here, we review the available mechanistic evidence and models that argue for the essential roles of calcium, calmodulin, and the Ca/calmodulin-dependent protein kinase II in integrating calcium signals to modulate the strength of electrical synapses through interactions with the gap junction protein .

摘要

在最初阶段,有关神经元之间存在缝隙连接和电耦联的解剖学和电生理学证据仅限于无脊椎动物和非哺乳动物,人们认为这是一种原始的突触传递形式。最近的研究表明,电通讯在哺乳动物中枢神经系统(CNS)中很常见,通常与化学突触传递共存。随后的研究进展表明,非哺乳动物中由缝隙连接蛋白连接蛋白-36()及其同源物形成的电突触是哺乳动物和鱼类突触回路的重要组成部分。它们控制着耦合神经元的集体活动,缝隙连接赋予它们巨大的适应性可塑性,就像在化学突触中看到的那样。此外,它们协调同步的神经元网络活动和节律性振荡,这些活动是基本整合过程的基础,如记忆和学习。在这里,我们回顾了现有的机制证据和模型,这些证据和模型表明钙、钙调蛋白和钙/钙调蛋白依赖性蛋白激酶 II 在整合钙信号方面的重要作用,通过与缝隙连接蛋白的相互作用来调节电突触的强度。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/32ccca55a49f/ijms-22-04473-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/a498922fb084/ijms-22-04473-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/40954446657e/ijms-22-04473-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/e5f43b3d4750/ijms-22-04473-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/32ccca55a49f/ijms-22-04473-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/a498922fb084/ijms-22-04473-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/40954446657e/ijms-22-04473-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/e5f43b3d4750/ijms-22-04473-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1c6b/8123330/32ccca55a49f/ijms-22-04473-g004.jpg

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