Journal
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
Volume 369, Issue 1633, Pages -Publisher
ROYAL SOC
DOI: 10.1098/rstb.2013.0144
Keywords
Alzheimer's disease; hippocampus; synaptic plasticity; long-term depression; tau
Categories
Funding
- National Center for Geriatrics and Gerontology [23-39]
- Strategic Research Programme for Brain Science ('Integrated Research on Neuropsychiatric Disorders')
- Ministry of Education, Science, Sports and Culture of Japan
- UK Wellcome Trust-MRC Neurodegenerative Disease Initiative Programme
- Korea-UK Alzheimer's Disease Research Consortium programme from the Ministry of Health and Welfare (Korea)
- WCU Programme (Korea)
- British Council
- Sasakawa Foundation
- Wolfson Research Merit Award
- Royal Society, London
- Ministry of Science, ICT & Future Planning, Republic of Korea [IBS-R002-D1-2014-A00] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2012R1A1A1044825] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Biotechnology and Biological Sciences Research Council [BB/G003963/1] Funding Source: researchfish
- Medical Research Council [984406, MC_G1000734, MR/K023098/1] Funding Source: researchfish
- BBSRC [BB/G003963/1] Funding Source: UKRI
- MRC [MC_G1000734, MR/K023098/1] Funding Source: UKRI
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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 in vivo and in vitro, an effect that was replicated by RNAi knockdown of tau in vitro. 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.
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