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哺乳动物突触的分子组织和调节由翻译后修饰 SUMOylation 完成。

Molecular Organization and Regulation of the Mammalian Synapse by the Post-Translational Modification SUMOylation.

机构信息

Université Côte d'Azur, CNRS, Inserm, IPMC, Sophia Antipolis, F-06560 Valbonne, France.

Centre for Discovery Brain Sciences, University of Edinburgh, Edinburgh EH8 9XD, UK.

出版信息

Cells. 2024 Feb 28;13(5):420. doi: 10.3390/cells13050420.

DOI:10.3390/cells13050420
PMID:38474384
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10930594/
Abstract

Neurotransmission occurs within highly specialized compartments forming the active synapse where the complex organization and dynamics of the interactions are tightly orchestrated both in time and space. Post-translational modifications (PTMs) are central to these spatiotemporal regulations to ensure an efficient synaptic transmission. SUMOylation is a dynamic PTM that modulates the interactions between proteins and consequently regulates the conformation, the distribution and the trafficking of the SUMO-target proteins. SUMOylation plays a crucial role in synapse formation and stabilization, as well as in the regulation of synaptic transmission and plasticity. In this review, we summarize the molecular consequences of this protein modification in the structural organization and function of the mammalian synapse. We also outline novel activity-dependent regulation and consequences of the SUMO process and explore how this protein modification can functionally participate in the compartmentalization of both pre- and post-synaptic sites.

摘要

神经传递发生在高度专业化的隔室中,这些隔室形成活跃的突触,其中相互作用的复杂组织和动力学在时间和空间上都被紧密协调。翻译后修饰 (PTM) 是这些时空调节的核心,以确保有效的突触传递。SUMOylation 是一种动态的 PTM,可调节蛋白质之间的相互作用,从而调节 SUMO 靶蛋白的构象、分布和运输。SUMOylation 在突触形成和稳定以及突触传递和可塑性的调节中起着至关重要的作用。在这篇综述中,我们总结了这种蛋白质修饰在哺乳动物突触的结构组织和功能中的分子后果。我们还概述了 SUMO 过程的新的活性依赖性调节及其后果,并探讨了这种蛋白质修饰如何在突触前和突触后位点的分区中发挥功能。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/d1a6a2d7cdb5/cells-13-00420-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/b03e95c832ca/cells-13-00420-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/135cff1cac70/cells-13-00420-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/b9288991bc48/cells-13-00420-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/0f8af16b6727/cells-13-00420-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/d1a6a2d7cdb5/cells-13-00420-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/b03e95c832ca/cells-13-00420-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/135cff1cac70/cells-13-00420-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/b9288991bc48/cells-13-00420-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/0f8af16b6727/cells-13-00420-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fde9/10930594/d1a6a2d7cdb5/cells-13-00420-g005.jpg

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