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      Myosin II ATPase Activity Mediates the Long-Term Potentiation-Induced Exodus of Stable F-Actin Bound by Drebrin A from Dendritic Spines

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          Abstract

          The neuronal actin-binding protein drebrin A forms a stable structure with F-actin in dendritic spines. NMDA receptor activation causes an exodus of F-actin bound by drebrin A (DA-actin) from dendritic spines, suggesting a pivotal role for DA-actin exodus in synaptic plasticity. We quantitatively assessed the extent of DA-actin localization to spines using the spine-dendrite ratio of drebrin A in cultured hippocampal neurons, and found that (1) chemical long-term potentiation (LTP) stimulation induces rapid DA-actin exodus and subsequent DA-actin re-entry in dendritic spines, (2) Ca 2+ influx through NMDA receptors regulates the exodus and the basal accumulation of DA-actin, and (3) the DA-actin exodus is blocked by myosin II ATPase inhibitor, but is not blocked by myosin light chain kinase (MLCK) or Rho-associated kinase (ROCK) inhibitors. These results indicate that myosin II mediates the interaction between NMDA receptor activation and DA-actin exodus in LTP induction. Furthermore, myosin II seems to be activated by a rapid actin-linked mechanism rather than slow MLC phosphorylation. Thus the myosin-II mediated DA-actin exodus might be an initial event in LTP induction, triggering actin polymerization and spine enlargement.

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          Long-term potentiation and memory.

          M A Lynch (2004)
          One of the most significant challenges in neuroscience is to identify the cellular and molecular processes that underlie learning and memory formation. The past decade has seen remarkable progress in understanding changes that accompany certain forms of acquisition and recall, particularly those forms which require activation of afferent pathways in the hippocampus. This progress can be attributed to a number of factors including well-characterized animal models, well-defined probes for analysis of cell signaling events and changes in gene transcription, and technology which has allowed gene knockout and overexpression in cells and animals. Of the several animal models used in identifying the changes which accompany plasticity in synaptic connections, long-term potentiation (LTP) has received most attention, and although it is not yet clear whether the changes that underlie maintenance of LTP also underlie memory consolidation, significant advances have been made in understanding cell signaling events that contribute to this form of synaptic plasticity. In this review, emphasis is focused on analysis of changes that occur after learning, especially spatial learning, and LTP and the value of assessing these changes in parallel is discussed. The effect of different stressors on spatial learning/memory and LTP is emphasized, and the review concludes with a brief analysis of the contribution of studies, in which transgenic animals were used, to the literature on memory/learning and LTP.
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            Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity.

            Ken-Ichi Okamoto, Takeharu Nagai, Atsushi Miyawaki … (2004)
            The synapse is a highly organized cellular specialization whose structure and composition are reorganized, both positively and negatively, depending on the strength of input signals. The mechanisms orchestrating these changes are not well understood. A plausible locus for the reorganization of synapse components and structure is actin, because it serves as both cytoskeleton and scaffold for synapses and exists in a dynamic equilibrium between F-actin and G-actin that is modulated bidirectionally by cellular signaling. Using a new FRET-based imaging technique to monitor F-actin/G-actin equilibrium, we show here that tetanic stimulation causes a rapid, persistent shift of actin equilibrium toward F-actin in the dendritic spines of rat hippocampal neurons. This enlarges the spines and increases postsynaptic binding capacity. In contrast, prolonged low-frequency stimulation shifts the equilibrium toward G-actin, resulting in a loss of postsynaptic actin and of structure. This bidirectional regulation of actin is actively involved in protein assembly and disassembly and provides a substrate for bidirectional synaptic plasticity.
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              Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo.

              Yugo Fukazawa, Yoshito Saitoh, Fumiko Ozawa … (2003)
              The dendritic spine is an important site of neuronal plasticity and contains extremely high levels of cytoskeletal actin. However, the dynamics of the actin cytoskeleton during synaptic plasticity and its in vivo function remain unclear. Here we used an in vivo dentate gyrus LTP model to show that LTP induction is associated with actin cytoskeletal reorganization characterized by a long-lasting increase in F-actin content within dendritic spines. This increase in F-actin content is dependent on NMDA receptor activation and involves the inactivation of actin depolymerizing factor/cofilin. Inhibition of actin polymerization with latrunculin A impaired late phase of LTP without affecting the initial amplitude and early maintenance of LTP. These observations suggest that mechanisms regulating the spine actin cytoskeleton contribute to the persistence of LTP.
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                Author and article information

                Contributors
                Makoto Sato: Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (iso-abbrev): PLoS ONE
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2014
                Publication date (Electronic): 22 January 2014
                Volume: 9
                Issue: 1
                Electronic Location Identifier: e85367
                Affiliations
                [1 ]Department of Neurobiology and Behavior, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan
                [2 ]Core Research for Evolution Science and Technology, Japan Science and Technology Corporation, Kawaguchi, Saitama, Japan
                [3 ]Bio-interface Research Group, Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka, Japan
                Osaka University Graduate School of Medicine, Japan
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Conceived and designed the experiments: TM YS TS. Performed the experiments: TM HY YI HT. Analyzed the data: TM YS HY YI HT NK MK. Wrote the paper: TM YS TS.

                [¤a]

                Current address: Division of Pharmacology, National Institute of Health Sciences, Setagaya-ku, Tokyo, Japan

                [¤b]

                Current address: Institut de recherches cliniques de Montréal (IRCM), Université de Montréal (UdeM), Québec, Canada

                Article
                Publisher ID: PONE-D-13-39922
                DOI: 10.1371/journal.pone.0085367
                PMC ID: 3899004
                PubMed ID: 24465547
                SO-VID: 9cae2d7c-2588-4be6-a30d-d9efc90b972e
                Copyright statement: Copyright @ 2014
                License:

                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 credited.

                History
                Date received : 30 September 2013
                Date accepted : 25 November 2013
                Page count
                Pages: 10
                Funding
                This work was supported by Grants-in-Aid for Scientific Research (16300117, 19200029) and on Priority Areas - Elucidation of neural network function in the brain - from the Ministry of Education, Culture, Sports, Science and Technology of Japan (20021002). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Subject: Research Article
                Subject: Biology
                Subject: Anatomy and Physiology
                Subject: Neurological System
                Subject: Neuroanatomy
                Subject: Biochemistry
                Subject: Neurochemistry
                Subject: Neurochemicals
                Subject: Neurotransmitters
                Subject: Synaptic Plasticity
                Subject: Proteins
                Subject: Structural Proteins
                Subject: Biophysics
                Subject: Cell Motility
                Subject: Actin Filaments
                Subject: Molecular Cell Biology
                Subject: Cellular Types
                Subject: Neurons
                Subject: Signal Transduction
                Subject: Signaling in Selected Disciplines
                Subject: Neurological Signaling
                Subject: Cellular Structures
                Subject: Neuroscience
                Subject: Cellular Neuroscience
                Subject: Neuronal Morphology
                Subject: Developmental Neuroscience
                Subject: Synaptic Plasticity
                Subject: Neurochemistry
                Subject: Neurochemicals
                Subject: Molecular Neuroscience
                Subject: Medicine
                Subject: Anatomy and Physiology
                Subject: Neurological System
                Subject: Neuroanatomy

                ScienceOpen disciplines: Uncategorized
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                ScienceOpen disciplines: Uncategorized

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