N-cofilin can compensate for the loss of ADF in excitatory synapses

Actin plays important roles in a number of synaptic processes, including synaptic vesicle organization and exocytosis, mobility of postsynaptic receptors, and synaptic plasticity. However, little is known about the mechanisms that control actin at synapses. Actin dynamics crucially depend on LIM kin...

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Published inPloS one Vol. 6; no. 10; p. e26789
Main Authors Görlich, Andreas, Wolf, Michael, Zimmermann, Anika-Maria, Gurniak, Christine B, Al Banchaabouchi, Mumna, Sassoè-Pognetto, Marco, Witke, Walter, Friauf, Eckhard, Rust, Marco B
Format Journal Article
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Published United States Public Library of Science 28.10.2011
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Abstract Actin plays important roles in a number of synaptic processes, including synaptic vesicle organization and exocytosis, mobility of postsynaptic receptors, and synaptic plasticity. However, little is known about the mechanisms that control actin at synapses. Actin dynamics crucially depend on LIM kinase 1 (LIMK1) that controls the activity of the actin depolymerizing proteins of the ADF/cofilin family. While analyses of mouse mutants revealed the importance of LIMK1 for both pre- and postsynaptic mechanisms, the ADF/cofilin family member n-cofilin appears to be relevant merely for postsynaptic plasticity, and not for presynaptic physiology. By means of immunogold electron microscopy and immunocytochemistry, we here demonstrate the presence of ADF (actin depolymerizing factor), a close homolog of n-cofilin, in excitatory synapses, where it is particularly enriched in presynaptic terminals. Surprisingly, genetic ablation of ADF in mice had no adverse effects on synapse structure or density as assessed by electron microscopy and by the morphological analysis of Golgi-stained hippocampal pyramidal cells. Moreover, a series of electrophysiological recordings in acute hippocampal slices revealed that presynaptic recruitment and exocytosis of synaptic vesicles as well as postsynaptic plasticity were unchanged in ADF mutant mice. The lack of synaptic defects may be explained by the elevated n-cofilin levels observed in synaptic structures of ADF mutants. Indeed, synaptic actin regulation was impaired in compound mutants lacking both ADF and n-cofilin, but not in ADF single mutants. From our results we conclude that n-cofilin can compensate for the loss of ADF in excitatory synapses. Further, our data suggest that ADF and n-cofilin cooperate in controlling synaptic actin content.
AbstractList Actin plays important roles in a number of synaptic processes, including synaptic vesicle organization and exocytosis, mobility of postsynaptic receptors, and synaptic plasticity. However, little is known about the mechanisms that control actin at synapses. Actin dynamics crucially depend on LIM kinase 1 (LIMK1) that controls the activity of the actin depolymerizing proteins of the ADF/cofilin family. While analyses of mouse mutants revealed the importance of LIMK1 for both pre- and postsynaptic mechanisms, the ADF/cofilin family member n-cofilin appears to be relevant merely for postsynaptic plasticity, and not for presynaptic physiology. By means of immunogold electron microscopy and immunocytochemistry, we here demonstrate the presence of ADF (actin depolymerizing factor), a close homolog of n-cofilin, in excitatory synapses, where it is particularly enriched in presynaptic terminals. Surprisingly, genetic ablation of ADF in mice had no adverse effects on synapse structure or density as assessed by electron microscopy and by the morphological analysis of Golgi-stained hippocampal pyramidal cells. Moreover, a series of electrophysiological recordings in acute hippocampal slices revealed that presynaptic recruitment and exocytosis of synaptic vesicles as well as postsynaptic plasticity were unchanged in ADF mutant mice. The lack of synaptic defects may be explained by the elevated n-cofilin levels observed in synaptic structures of ADF mutants. Indeed, synaptic actin regulation was impaired in compound mutants lacking both ADF and n-cofilin, but not in ADF single mutants. From our results we conclude that n-cofilin can compensate for the loss of ADF in excitatory synapses. Further, our data suggest that ADF and n-cofilin cooperate in controlling synaptic actin content.
Actin plays important roles in a number of synaptic processes, including synaptic vesicle organization and exocytosis, mobility of postsynaptic receptors, and synaptic plasticity. However, little is known about the mechanisms that control actin at synapses. Actin dynamics crucially depend on LIM kinase 1 (LIMK1) that controls the activity of the actin depolymerizing proteins of the ADF/cofilin family. While analyses of mouse mutants revealed the importance of LIMK1 for both pre- and postsynaptic mechanisms, the ADF/cofilin family member n-cofilin appears to be relevant merely for postsynaptic plasticity, and not for presynaptic physiology. By means of immunogold electron microscopy and immunocytochemistry, we here demonstrate the presence of ADF ( a ctin d epolymerizing f actor), a close homolog of n-cofilin, in excitatory synapses, where it is particularly enriched in presynaptic terminals. Surprisingly, genetic ablation of ADF in mice had no adverse effects on synapse structure or density as assessed by electron microscopy and by the morphological analysis of Golgi-stained hippocampal pyramidal cells. Moreover, a series of electrophysiological recordings in acute hippocampal slices revealed that presynaptic recruitment and exocytosis of synaptic vesicles as well as postsynaptic plasticity were unchanged in ADF mutant mice. The lack of synaptic defects may be explained by the elevated n-cofilin levels observed in synaptic structures of ADF mutants. Indeed, synaptic actin regulation was impaired in compound mutants lacking both ADF and n-cofilin, but not in ADF single mutants. From our results we conclude that n-cofilin can compensate for the loss of ADF in excitatory synapses. Further, our data suggest that ADF and n-cofilin cooperate in controlling synaptic actin content.
Audience Academic
Author Gurniak, Christine B
Wolf, Michael
Al Banchaabouchi, Mumna
Görlich, Andreas
Sassoè-Pognetto, Marco
Rust, Marco B
Friauf, Eckhard
Witke, Walter
Zimmermann, Anika-Maria
AuthorAffiliation 5 Animal Physiology Group, University of Kaiserslautern, Kaiserslautern, Germany
2 Institute of Genetics, University of Bonn, Bonn, Germany
3 Mouse Biology Unit, European Mouse Biology Laboratory, Monterotondo, Italy
University of Houston, United States of America
1 Neurobiology/Neurophysiology Group, University of Kaiserslautern, Kaiserslautern, Germany
4 Department of Anatomy, Pharmacology and Forensic Medicine and National Institute of Neuroscience-Italy, University of Turin, Turin, Italy
AuthorAffiliation_xml – name: 2 Institute of Genetics, University of Bonn, Bonn, Germany
– name: 5 Animal Physiology Group, University of Kaiserslautern, Kaiserslautern, Germany
– name: 1 Neurobiology/Neurophysiology Group, University of Kaiserslautern, Kaiserslautern, Germany
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– name: 3 Mouse Biology Unit, European Mouse Biology Laboratory, Monterotondo, Italy
– name: 4 Department of Anatomy, Pharmacology and Forensic Medicine and National Institute of Neuroscience-Italy, University of Turin, Turin, Italy
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/22046357$$D View this record in MEDLINE/PubMed
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2011 Görlich et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Görlich et al. 2011
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– notice: 2011 Görlich et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
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Conceived and designed the experiments: MBR EF WW MSP. Performed the experiments: AG MW AMZ MBR CBG MA. Analyzed the data: AG MW AMZ MBR MA. Contributed reagents/materials/analysis tools: CBG WW. Wrote the paper: MBR EF WW AG MSP.
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Snippet Actin plays important roles in a number of synaptic processes, including synaptic vesicle organization and exocytosis, mobility of postsynaptic receptors, and...
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StartPage e26789
SubjectTerms Actin
Actins - metabolism
Animals
Biology
Brain
Cell culture
Cell cycle
Cofilin
Cofilin 1 - metabolism
Cofilin 1 - physiology
Depolymerization
Destrin - deficiency
Destrin - metabolism
Electron microscopy
Exocytosis
Experiments
Hippocampus
Hippocampus - cytology
Hippocampus - physiology
Homology
Immunocytochemistry
Immunoglobulins
Immunohistochemistry
Laboratory animals
Leukemia
LIM kinase
Lim Kinases
Memory
Mice
Microscopy, Electron
Morphology
Muscle proteins
Mutants
Neurobiology
Neurons
Neurosciences
Phosphorylation
Physiological aspects
Physiology
Plasticity
Presynaptic plasticity
Presynaptic Terminals
Proteins
Pyramidal cells
Pyramidal Cells - physiology
Receptors
Rodents
Synapses
Synaptic plasticity
Synaptic vesicles
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Title N-cofilin can compensate for the loss of ADF in excitatory synapses
URI https://www.ncbi.nlm.nih.gov/pubmed/22046357
https://www.proquest.com/docview/1309933467
https://search.proquest.com/docview/902086383
https://pubmed.ncbi.nlm.nih.gov/PMC3203908
https://doaj.org/article/1ce53aeb0ed04f3c9881bd234b7fe7dc
http://dx.doi.org/10.1371/journal.pone.0026789
Volume 6
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