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    • Microtubule-associated protein tau is essential for long-term depression in the hippocampus

    DOI HANDLE HANDLE HANDLE Web Site ほか2件をすべて表示 一部だけ表示 研究データあり 被引用文献14件 参考文献40件 オープンアクセス
    • Tetsuya Kimura
      Department of Aging Neurobiology, Center for Development of Advanced Medicine for Dementia, National Center for Geriatrics and Gerontology, 35 Gengo, Morioka, Obu, Aichi 474-8522, Japan
    • Daniel J. Whitcomb
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Jihoon Jo
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Philip Regan
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Thomas Piers
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Seonghoo Heo
      Chonnam-Bristol Frontier Laboratory, Biomedical Research Institute, Chonnam National University Hospital, Gwangju 501-757, South Korea
    • Christopher Brown
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Tsutomu Hashikawa
      Laboratory for Alzheimer's Disease, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan
    • Miyuki Murayama
      Laboratory for Alzheimer's Disease, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan
    • Heon Seok
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Ioannis Sotiropoulos
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Eunjoon Kim
      Center for Synaptic Brain Dysfunctions, Institute for Basic Science and Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, South Korea
    • Graham L. Collingridge
      Centre for Synaptic Plasticity, University of Bristol, University Walk, Bristol BS8 1TD, UK
    • Akihiko Takashima
      Department of Aging Neurobiology, Center for Development of Advanced Medicine for Dementia, National Center for Geriatrics and Gerontology, 35 Gengo, Morioka, Obu, Aichi 474-8522, Japan
    • Kwangwook Cho
      Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, UK
    • Universidade do Minho

    書誌事項

    公開日
    2014-01-05
    資源種別
    journal article
    権利情報
    • https://royalsociety.org/journals/ethics-policies/data-sharing-mining/
    DOI
    • 10.1098/rstb.2013.0144
    公開者
    The Royal Society

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    説明

    <jats:p> The microtubule-associated protein tau is a principal component of neurofibrillary tangles, and has been identified as a key molecule in Alzheimer's disease and other tauopathies. However, it is unknown how a protein that is primarily located in axons is involved in a disease that is believed to have a synaptic origin. To investigate a possible synaptic function of tau, we studied synaptic plasticity in the hippocampus and found a selective deficit in long-term depression (LTD) in tau knockout mice <jats:italic>in vivo</jats:italic> and <jats:italic>in vitro</jats:italic> , an effect that was replicated by RNAi knockdown of tau <jats:italic>in vitro</jats:italic> . We found that the induction of LTD is associated with the glycogen synthase kinase-3-mediated phosphorylation of tau. These observations demonstrate that tau has a critical physiological function in LTD. </jats:p>

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