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...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24853857/?tool=EBI |
| _version_ | 1819100699503362048 |
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| author | Zsuzsanna Szepesi Eric Hosy Blazej Ruszczycki Monika Bijata Marta Pyskaty Arthur Bikbaev Martin Heine Daniel Choquet Leszek Kaczmarek Jakub Wlodarczyk |
| author_facet | Zsuzsanna Szepesi Eric Hosy Blazej Ruszczycki Monika Bijata Marta Pyskaty Arthur Bikbaev Martin Heine Daniel Choquet Leszek Kaczmarek Jakub Wlodarczyk |
| author_sort | Zsuzsanna Szepesi |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-22T01:06:56Z |
| format | Article |
| id | doaj.art-dc4744a825bd4ffb92a38ab7ed2c89cc |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T01:06:56Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-dc4744a825bd4ffb92a38ab7ed2c89cc2022-12-21T18:44:03ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0195e9827410.1371/journal.pone.0098274Synaptically released matrix metalloproteinase activity in control of structural plasticity and the cell surface distribution of GluA1-AMPA receptors.Zsuzsanna SzepesiEric HosyBlazej RuszczyckiMonika BijataMarta PyskatyArthur BikbaevMartin HeineDaniel ChoquetLeszek KaczmarekJakub WlodarczykSynapses 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24853857/?tool=EBI |
| spellingShingle | Zsuzsanna Szepesi Eric Hosy Blazej Ruszczycki Monika Bijata Marta Pyskaty Arthur Bikbaev Martin Heine Daniel Choquet Leszek Kaczmarek Jakub Wlodarczyk Synaptically released matrix metalloproteinase activity in control of structural plasticity and the cell surface distribution of GluA1-AMPA receptors. PLoS ONE |
| title | 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_short | 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 |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24853857/?tool=EBI |
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