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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
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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. |
format | Online Article Text |
id | pubmed-6753054 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
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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