Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors

Synapses are particularly prone to dynamic alterations and thus play a major role in neuronal plasticity. Dynamic excitatory synapses are located at the membranous neuronal protrusions called dendritic spines. The ability to change synaptic connections involves both alterations at the morphological...

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Main Authors:	Szepesi, Zsuzsanna, Hosy, Eric, Ruszczycki, Blazej, Bijata, Monika, Pyskaty, Marta, Bikbaev, Arthur, Heine, Martin, Choquet, Daniel, Kaczmarek, Leszek, Wlodarczyk, Jakub
Format:	Online
Language:	English
Published:	Public Library of Science 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4031140/

id	pubmed-4031140
recordtype	oai_dc
spelling	pubmed-40311402014-05-28 Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors Szepesi, Zsuzsanna Hosy, Eric Ruszczycki, Blazej Bijata, Monika Pyskaty, Marta Bikbaev, Arthur Heine, Martin Choquet, Daniel Kaczmarek, Leszek Wlodarczyk, Jakub Research Article Synapses are particularly prone to dynamic alterations and thus play a major role in neuronal plasticity. Dynamic excitatory synapses are located at the membranous neuronal protrusions called dendritic spines. The ability to change synaptic connections involves both alterations at the morphological level and changes in postsynaptic receptor composition. We report that endogenous matrix metalloproteinase (MMP) activity promotes the structural and functional plasticity of local synapses by its effect on glutamate receptor mobility and content. We used live imaging of cultured hippocampal neurons and quantitative morphological analysis to show that chemical long-term potentiation (cLTP) induces the permanent enlargement of a subset of small dendritic spines in an MMP-dependent manner. We also used a superresolution microscopy approach and found that spine expansion induced by cLTP was accompanied by MMP-dependent immobilization and synaptic accumulation as well as the clustering of GluA1-containing AMPA receptors. Altogether, our results reveal novel molecular and cellular mechanisms of synaptic plasticity. Public Library of Science 2014-05-22 /pmc/articles/PMC4031140/ /pubmed/24853857 http://dx.doi.org/10.1371/journal.pone.0098274 Text en © 2014 Szepesi et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Szepesi, Zsuzsanna Hosy, Eric Ruszczycki, Blazej Bijata, Monika Pyskaty, Marta Bikbaev, Arthur Heine, Martin Choquet, Daniel Kaczmarek, Leszek Wlodarczyk, Jakub
spellingShingle	Szepesi, Zsuzsanna Hosy, Eric Ruszczycki, Blazej Bijata, Monika Pyskaty, Marta Bikbaev, Arthur Heine, Martin Choquet, Daniel Kaczmarek, Leszek Wlodarczyk, Jakub Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors
author_facet	Szepesi, Zsuzsanna Hosy, Eric Ruszczycki, Blazej Bijata, Monika Pyskaty, Marta Bikbaev, Arthur Heine, Martin Choquet, Daniel Kaczmarek, Leszek Wlodarczyk, Jakub
author_sort	Szepesi, Zsuzsanna
title	Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors
title_short	Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors
title_full	Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors
title_fullStr	Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors
title_full_unstemmed	Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors
title_sort	synaptically released matrix metalloproteinase activity in control of structural plasticity and the cell surface distribution of glua1-ampa receptors
description	Synapses are particularly prone to dynamic alterations and thus play a major role in neuronal plasticity. Dynamic excitatory synapses are located at the membranous neuronal protrusions called dendritic spines. The ability to change synaptic connections involves both alterations at the morphological level and changes in postsynaptic receptor composition. We report that endogenous matrix metalloproteinase (MMP) activity promotes the structural and functional plasticity of local synapses by its effect on glutamate receptor mobility and content. We used live imaging of cultured hippocampal neurons and quantitative morphological analysis to show that chemical long-term potentiation (cLTP) induces the permanent enlargement of a subset of small dendritic spines in an MMP-dependent manner. We also used a superresolution microscopy approach and found that spine expansion induced by cLTP was accompanied by MMP-dependent immobilization and synaptic accumulation as well as the clustering of GluA1-containing AMPA receptors. Altogether, our results reveal novel molecular and cellular mechanisms of synaptic plasticity.
publisher	Public Library of Science
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4031140/
_version_	1612092384413220864

Synaptically Released Matrix Metalloproteinase Activity in Control of Structural Plasticity and the Cell Surface Distribution of GluA1-AMPA Receptors

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