Evidence map›Paper›PMID 23197718›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012

SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease.

Yi Hong, Chi Bun Chan, Il-Sun Kwon, Xuekun Li, Mingke Song, Hyun-Pil Lee, Xia Liu, Pradoldej Sompol, Peng Jin, Hyoung-gon Lee and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 2 pooled it
1.7field-weighted citation impact, top 17% 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

41 citing papers in PubMed, 2 syntheses or guidelines pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  12. Clinical and genetic analysis of a case of OZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2024
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  18. The Mammalian Cysteine Protease Legumain in Health and Disease.International journal of molecular sciences · 2022
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 1 country.

Yi HongDepartment of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Chi Bun Chan
Il-Sun Kwon
Xuekun Li
Mingke Song
Hyun-Pil Lee
Xia Liu
Pradoldej Sompol
Peng Jin
Hyoung-gon Lee
Shan Ping Yu
Keqiang Ye
Emory University · USUniversity School · US

Funding

The Emory Alzheimer's Disease CenterP50AG025688 · NIA · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2005 to 2019
$25.7M
Molecular Basis of rCGG-Mediated NeurodegenerationR01NS051630 · NINDS · EMORY UNIVERSITY · PI NELSON, DAVID LOREN · 2006 to 2023
$9.8M
Phosphorylation of Acinus Regulates its Biological FunctionsR01NS060680 · NINDS · EMORY UNIVERSITY · PI YE, KEQIANG · 2009 to 2013
$1.7M
Role of Cell Cycle in NeurodegenerationR01AG028679 · NIA · CASE WESTERN RESERVE UNIVERSITY · PI LEE, HYOUNG-GON · 2008 to 2012
$1.6M
NIA NIH HHS AG028679NIA NIH HHS P50 AG025688NIA NIH HHS R01 AG028679NINDS NIH HHS NS060680NINDS NIH HHS R01 NS051630NINDS NIH HHS R01 NS060680
6 · The paper itself

Abstract

Serine-arginine protein kinases 2 (SRPK2) is a cell cycle-regulated kinase that phosphorylates serine/arginine domain-containing proteins and mediates pre-mRNA splicing with unclear function in neurons. Here, we show that SRPK2 phosphorylates tau on S214, suppresses tau-dependent microtubule polymerization, and inhibits axonal elongation in neurons. Depletion of SRPK2 in dentate gyrus inhibits tau phosphorylation in APP/PS1 mouse and alleviates the impaired cognitive behaviors. The defective LTP in APP/PS1 mice is also improved after SRPK2 depletion. Moreover, active SRPK2 is increased in the cortex of APP/PS1 mice and the pathological structures of human Alzheimer's disease (AD) brain. Therefore, our study suggests SRPK2 may contribute to the formation of hyperphosphorylated tau and the pathogenesis of AD.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsBehavior, AnimalBrainDisease Models, AnimalHumansMaze LearningMiceMice, TransgenicNeuritesNeuronal PlasticityNeuronsPhosphorylationPresenilin-1Protein Serine-Threonine KinasesAmyloid beta-Protein PrecursorPresenilin-1Protein Serine-Threonine KinasesSrpk2 protein, mousetau Proteins

Identifiers

PMID23197718
PMCPMC3518045
OpenAlexW2054983851

What OpenQuestion holds

Textmetadata
LicenceTDM
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.