Evidence map›Paper›PMID 27041503›Full record

ArticleNeuron2016

Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss.

Tara E Tracy, Peter Dongmin Sohn, S Sakura Minami, Chao Wang, Sang-Won Min, Yaqiao Li, Yungui Zhou, David Le, Iris Lo, Ravikumar Ponnusamy and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Neuron, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 168 papers.

0numbers the graph read from it
0cells of the map it votes in
168citing papers in PubMed
26.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

168 citing papers in PubMed, 271 citations in OpenAlex.

  1. Review
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  12. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
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  16. Review
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108 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 4 institutions in 1 country.

Tara E TracyGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA; Department of Neurology, University of California, San Francisco, San Francisco, CA 91458, USA.
Peter Dongmin SohnGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA; Neuroscience Graduate Program, University of California, San Francisco, San Francisco, CA 91458, USA.
S Sakura MinamiGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA; Department of Neurology, University of California, San Francisco, San Francisco, CA 91458, USA.
Chao WangGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA; Department of Neurology, University of California, San Francisco, San Francisco, CA 91458, USA.
Sang-Won MinGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA; Department of Neurology, University of California, San Francisco, San Francisco, CA 91458, USA.
Yaqiao LiGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA.
Yungui ZhouGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA.
David LeGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA.
Iris LoGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA.
Ravikumar PonnusamyGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA.
Xin CongBuck Institute for Research on Aging, Novato, CA 94945, USA.
Birgit SchillingBuck Institute for Research on Aging, Novato, CA 94945, USA.
Lisa M EllerbyBuck Institute for Research on Aging, Novato, CA 94945, USA.
Richard L HuganirDepartment of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Li GanGladstone Institute of Neurological Disease, San Francisco, CA 91458, USA; Department of Neurology, University of California, San Francisco, San Francisco, CA 91458, USA; Neuroscience Graduate Program, University of California, San Francisco, San Francisco, CA 91458, USA. Electronic address: lgan@gladstone.ucsf.edu.
Gladstone Institutes · USBuck Institute for Research on Aging · USUniversity of California, San Francisco · USJohns Hopkins University · US

Funding

PDZ DOMAINS AND EXCITATORY SYNAPTIC FUNCTIONR01NS036715 · NINDS · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 1997 to 2020
$8.6M
Behavioral CoreP30NS065780 · NINDS · J. DAVID GLADSTONE INSTITUTES · PI MUCKE, LENNART · 2011 to 2015
$4.0M
TRIPLET REPEAT DISEASE: REQUIREMENT FOR CASPASE CLEAVAGER01NS040251 · NINDS · BUCK INSTITUTE FOR RESEARCH ON AGING · PI ELLERBY, LISA M. · 1999 to 2007
$3.1M
Molecular mechanisms in progranulin deficient frontotemporal dementiaR01AG051390 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI GAN, LI · 2015 to 2019
$2.5M
HDACs in Neurodegeneration and AgingRL1NS062413 · NINDS · BUCK INSTITUTE FOR RESEARCH ON AGING · PI ELLERBY, LISA M · 2007 to 2011
$2.3M
EXTRAMULAR RESEARCH FACILITIES CONSTRUCTIONC06RR018928 · NCRR · J. DAVID GLADSTONE INSTITUTES · PI MAHLEY, ROBERT W. · 2003 to 2003
$2.1M
SIRT1 Limits Microglial Toxicity in Alzheimer's DiseaseR01AG036884 · NIA · J. DAVID GLADSTONE INSTITUTES · PI GAN, LI · 2012 to 2016
$2.0M
The Role of Cathepsin B and Cystatin C in Alzheimer's DiseaseR01AG030207 · NIA · J. DAVID GLADSTONE INSTITUTES · PI GAN, LI · 2010 to 2014
$1.9M
Pathogenic events triggered by tau acetylation in neurodegenerative tauopathyF32AG043301 · NIA · J. DAVID GLADSTONE INSTITUTES · PI TRACY, TARA · 2012 to 2014
$156k
NCRR NIH HHS C06 RR018928NIA NIH HHS F32 AG043301NIA NIH HHS R01 AG030207NIA NIH HHS R01 AG036884NIA NIH HHS R01 AG051390NINDS NIH HHS P30 NS065780NINDS NIH HHS R01 NS036715NINDS NIH HHS R01 NS040251NINDS NIH HHS RL1 NS062413
6 · The paper itself

Abstract

Tau toxicity has been implicated in the emergence of synaptic dysfunction in Alzheimer's disease (AD), but the mechanism by which tau alters synapse physiology and leads to cognitive decline is unclear. Here we report abnormal acetylation of K274 and K281 on tau, identified in AD brains, promotes memory loss and disrupts synaptic plasticity by reducing postsynaptic KIdney/BRAin (KIBRA) protein, a memory-associated protein. Transgenic mice expressing human tau with lysine-to-glutamine mutations to mimic K274 and K281 acetylation (tauKQ) exhibit AD-related memory deficits and impaired hippocampal long-term potentiation (LTP). TauKQ reduces synaptic KIBRA levels and disrupts activity-induced postsynaptic actin remodeling and AMPA receptor insertion. The LTP deficit was rescued by promoting actin polymerization or by KIBRA expression. In AD patients with dementia, we found enhanced tau acetylation is linked to loss of KIBRA. These findings suggest a novel mechanism by which pathogenic tau causes synaptic dysfunction and cognitive decline in AD pathogenesis.

Indexed as

Signal TransductionAcetylationActinsAlzheimer DiseaseAnimalsBrainCarrier ProteinsHippocampusHumansIntracellular Signaling Peptides and ProteinsLong-Term PotentiationMemory DisordersMiceMice, TransgenicNeuronal PlasticityPhosphoproteinsActinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsPhosphoproteinsReceptors, AMPAtau ProteinsWwc1 protein, mouse

Identifiers

PMID27041503
PMCPMC4859346
OpenAlexW2327032644

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.