Synaptically released matrix metalloproteinase activity in control of structural plasticity and the cell surface distribution of GluA1-AMPA receptors.

Zsuzsanna Szepesi, Eric Hosy, Blazej Ruszczycki, Monika Bijata, Marta Pyskaty, Arthur Bikbaev, Martin Heine, Daniel Choquet, Leszek Kaczmarek, Jakub Wlodarczyk
PLoS ONE. 2014-05-22; 9(5): e98274
DOI: 10.1371/journal.pone.0098274

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1. PLoS One. 2014 May 22;9(5):e98274. doi: 10.1371/journal.pone.0098274. eCollection
2014.

Synaptically released matrix metalloproteinase activity in control of structural
plasticity and the cell surface distribution of GluA1-AMPA receptors.

Szepesi Z(1), Hosy E(2), Ruszczycki B(1), Bijata M(1), Pyskaty M(1), Bikbaev
A(3), Heine M(3), Choquet D(2), Kaczmarek L(1), Wlodarczyk J(1).

Author information:
(1)Department of Molecular and Cellular Neurobiology, Nencki Institute, Warsaw,
Poland.
(2)Dynamic Organization and Function of Synapses, Interdisciplinary Institute for
Neuroscience, Bordeaux, France.
(3)Department of Neurochemistry and Molecular Biology, Leibniz Institute for
Neurobiology, Magdeburg, Germany.

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.

DOI: 10.1371/journal.pone.0098274
PMCID: PMC4031140
PMID: 24853857 [Indexed for MEDLINE]

Auteurs Bordeaux Neurocampus