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Postsynaptic protein organization revealed by electron microscopy

Neuronal synapses are key devices for transmitting and processing information in the nervous system. Synaptic plasticity, generally regarded as the cellular basis of learning and memory, involves changes of subcellular structures that take place at the nanoscale. High-resolution imaging methods, esp...

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Detalles Bibliográficos
Autores principales: Liu, Yun-Tao, Tao, Chang-Lu, Lau, Pak-Ming, Zhou, Z Hong, Bi, Guo-Qiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6753054/
https://www.ncbi.nlm.nih.gov/pubmed/30904821
http://dx.doi.org/10.1016/j.sbi.2019.02.012
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author Liu, Yun-Tao
Tao, Chang-Lu
Lau, Pak-Ming
Zhou, Z Hong
Bi, Guo-Qiang
author_facet Liu, Yun-Tao
Tao, Chang-Lu
Lau, Pak-Ming
Zhou, Z Hong
Bi, Guo-Qiang
author_sort Liu, Yun-Tao
collection PubMed
description Neuronal synapses are key devices for transmitting and processing information in the nervous system. Synaptic plasticity, generally regarded as the cellular basis of learning and memory, involves changes of subcellular structures that take place at the nanoscale. High-resolution imaging methods, especially electron microscopy (EM), have allowed for quantitative analysis of such nanoscale structures in different types of synapses. In particular, the semi-ordered organization of neurotransmitter receptors and their interacting scaffolds in the postsynaptic density have been characterized for both excitatory and inhibitory synapses by studies using various EM techniques such as immuno-EM, electron tomography of high-pressure freezing and freeze-substituted samples, and cryo electron tomography. These techniques, in combination with new correlative approaches, will further facilitate our understanding of the molecular organization underlying diverse functions of neuronal synapses.
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spelling pubmed-67530542019-09-19 Postsynaptic protein organization revealed by electron microscopy Liu, Yun-Tao Tao, Chang-Lu Lau, Pak-Ming Zhou, Z Hong Bi, Guo-Qiang Curr Opin Struct Biol Article Neuronal synapses are key devices for transmitting and processing information in the nervous system. Synaptic plasticity, generally regarded as the cellular basis of learning and memory, involves changes of subcellular structures that take place at the nanoscale. High-resolution imaging methods, especially electron microscopy (EM), have allowed for quantitative analysis of such nanoscale structures in different types of synapses. In particular, the semi-ordered organization of neurotransmitter receptors and their interacting scaffolds in the postsynaptic density have been characterized for both excitatory and inhibitory synapses by studies using various EM techniques such as immuno-EM, electron tomography of high-pressure freezing and freeze-substituted samples, and cryo electron tomography. These techniques, in combination with new correlative approaches, will further facilitate our understanding of the molecular organization underlying diverse functions of neuronal synapses. 2019-03-21 2019-02 /pmc/articles/PMC6753054/ /pubmed/30904821 http://dx.doi.org/10.1016/j.sbi.2019.02.012 Text en This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Liu, Yun-Tao
Tao, Chang-Lu
Lau, Pak-Ming
Zhou, Z Hong
Bi, Guo-Qiang
Postsynaptic protein organization revealed by electron microscopy
title Postsynaptic protein organization revealed by electron microscopy
title_full Postsynaptic protein organization revealed by electron microscopy
title_fullStr Postsynaptic protein organization revealed by electron microscopy
title_full_unstemmed Postsynaptic protein organization revealed by electron microscopy
title_short Postsynaptic protein organization revealed by electron microscopy
title_sort postsynaptic protein organization revealed by electron microscopy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6753054/
https://www.ncbi.nlm.nih.gov/pubmed/30904821
http://dx.doi.org/10.1016/j.sbi.2019.02.012
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