The actin-binding protein profilin I is localized at synaptic sites in an activity-regulated manner

Morphological changes at synaptic specializations have been implicated in regulating synaptic strength. Actin turnover at dendritic spines is regulated by neuronal activity and contributes to spine size, shape and motility. The reorganization of actin filaments requires profilins, which stimulate ac...

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Veröffentlicht in:The European journal of neuroscience 2005-01, Vol.21 (1), p.15-25
Hauptverfasser: Neuhoff, Henrike, Sassoè-Pognetto, Marco, Panzanelli, Patrizia, Maas, Christoph, Witke, Walter, Kneussel, Matthias
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container_title The European journal of neuroscience
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creator Neuhoff, Henrike
Sassoè-Pognetto, Marco
Panzanelli, Patrizia
Maas, Christoph
Witke, Walter
Kneussel, Matthias
description Morphological changes at synaptic specializations have been implicated in regulating synaptic strength. Actin turnover at dendritic spines is regulated by neuronal activity and contributes to spine size, shape and motility. The reorganization of actin filaments requires profilins, which stimulate actin polymerization. Neurons express two independent gene products − profilin I and profilin II. A role for profilin II in activity‐dependent mechanisms at spine synapses has recently been described. Although profilin I interacts with synaptic proteins, little is known about its cellular and subcellular localization in neurons. Here, we investigated the subcellular distribution of this protein in brain neurons as well as in hippocampal cultures. Our results indicate that the expression of profilin I varies in different brain regions. Thus, in cerebral cortex and hippocampus profilin I immunostaining was associated predominantly with dendrites and was present in a subset of dendritic spines. In contrast, profilin I in cerebellum was associated primarily with presynaptic structures. Profilin I immunoreactivity was partially colocalized with the synaptic molecules synaptophysin, PSD‐95 and gephyrin in cultured hippocampal neurons, indicating that profilin I is present in only a subset of synapses. At dendritic spine structures, profilin I was found primarily in protrusions, which were in apposition to presynaptic terminal boutons. Remarkably, depolarization with KCl caused a moderate but significant increase in the number of synapses containing profilin I. These results show that profilin I can be present at both pre‐ and postsynaptic sites and suggest a role for this actin‐binding protein in activity‐dependent remodelling of synaptic structure.
doi_str_mv 10.1111/j.1460-9568.2004.03814.x
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Actin turnover at dendritic spines is regulated by neuronal activity and contributes to spine size, shape and motility. The reorganization of actin filaments requires profilins, which stimulate actin polymerization. Neurons express two independent gene products − profilin I and profilin II. A role for profilin II in activity‐dependent mechanisms at spine synapses has recently been described. Although profilin I interacts with synaptic proteins, little is known about its cellular and subcellular localization in neurons. Here, we investigated the subcellular distribution of this protein in brain neurons as well as in hippocampal cultures. Our results indicate that the expression of profilin I varies in different brain regions. Thus, in cerebral cortex and hippocampus profilin I immunostaining was associated predominantly with dendrites and was present in a subset of dendritic spines. In contrast, profilin I in cerebellum was associated primarily with presynaptic structures. Profilin I immunoreactivity was partially colocalized with the synaptic molecules synaptophysin, PSD‐95 and gephyrin in cultured hippocampal neurons, indicating that profilin I is present in only a subset of synapses. At dendritic spine structures, profilin I was found primarily in protrusions, which were in apposition to presynaptic terminal boutons. Remarkably, depolarization with KCl caused a moderate but significant increase in the number of synapses containing profilin I. These results show that profilin I can be present at both pre‐ and postsynaptic sites and suggest a role for this actin‐binding protein in activity‐dependent remodelling of synaptic structure.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15654839</pmid><doi>10.1111/j.1460-9568.2004.03814.x</doi><tpages>11</tpages></addata></record>
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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects actin
activity-dependent
Adaptor Proteins, Signal Transducing - metabolism
alpha Catenin
Animals
Animals, Newborn
Brain - anatomy & histology
Brain - metabolism
Carrier Proteins - metabolism
Cell Count - methods
Cells, Cultured
Contractile Proteins - metabolism
Cytoskeletal Proteins - metabolism
dendritic spine
Dendritic Spines - drug effects
Dendritic Spines - metabolism
Dendritic Spines - ultrastructure
Disks Large Homolog 4 Protein
Gene Expression Regulation - drug effects
Gene Expression Regulation - physiology
Green Fluorescent Proteins - metabolism
Guanylate Kinases
Hippocampus - cytology
Hippocampus - metabolism
Immunohistochemistry - methods
Intracellular Signaling Peptides and Proteins
Membrane Proteins - metabolism
Mice
Mice, Inbred C57BL
Microfilament Proteins - metabolism
Microscopy, Immunoelectron - methods
Nerve Tissue Proteins - metabolism
Neuronal Plasticity - drug effects
Neuronal Plasticity - physiology
Neurons - cytology
Neurons - drug effects
Neurons - metabolism
Potassium Chloride - pharmacology
profilin
Profilins
Statistics, Nonparametric
synapse
Synapses - drug effects
Synapses - metabolism
Synapses - ultrastructure
Synaptophysin - metabolism
title The actin-binding protein profilin I is localized at synaptic sites in an activity-regulated manner
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