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

Tetsuya Kimura | Zendy; Daniel J. Whitcomb | Zendy; Jihoon Jo | Zendy; Philip Regan | Zendy; Thomas M. Piers | Zendy; Seonghoo Heo | Zendy; Christopher Brown | Zendy; Tsutomu Hashikawa | Zendy; Miyuki Murayama | Zendy; Heon Seok | Zendy; Ioannis Sotiropoulos | Zendy; Eunjoon Kim | Zendy; Graham L. Collingridge | Zendy; Akihiko Takashima | Zendy; Kwangwook Cho | Zendy

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

Author(s) -

Tetsuya Kimura,

Daniel J. Whitcomb,

Jihoon Jo,

Philip Regan,

Thomas M. Piers,

Seonghoo Heo,

Christopher Brown,

Tsutomu Hashikawa,

Miyuki Murayama,

Heon Seok,

Ioannis Sotiropoulos,

Eunjoon Kim,

Graham L. Collingridge,

Akihiko Takashima,

Kwangwook Cho

Publication year - 2013

Publication title -

philosophical transactions of the royal society b biological sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.753

H-Index - 272

eISSN - 1471-2970

pISSN - 0962-8436

DOI - 10.1098/rstb.2013.0144

Subject(s) - hippocampus , depression (economics) , neuroscience , microtubule , term (time) , biology , long term depression , tau protein , microtubule associated protein , psychology , medicine , microbiology and biotechnology , genetics , alzheimer's disease , disease , glutamate receptor , physics , receptor , quantum mechanics , economics , ampa receptor , macroeconomics

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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