Evidence map›Paper›PMID 34290082›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2021

Regulation of Synapse Weakening through Interactions of the Microtubule Associated Protein Tau with PACSIN1.

Philip Regan, Scott J Mitchell, Seung-Chan Kim, Younbok Lee, Jee Hyun Yi, Saviana A Barbati, Christopher Shaw, Kwangwook Cho

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  4. Article
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  8. Article
  9. NMDARs in Alzheimer's Disease: Between Synaptic and Extrasynaptic Membranes.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Review
  12. Review
  13. Blood DNA Methylation Patterns in Older Adults With Evolving Dementia.The journals of gerontology. Series A, Biological sciences and medical sciences · 2022
    Article
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

8 authors at 3 institutions in 1 country.

Philip ReganHenry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, Bristol Medical School, Faculty of Health Sciences, University of Bristol, Bristol BS1 3NY, United Kingdom.
Scott J MitchellUK-Dementia Research Institute, Department of Basic and Clinical Neuroscience, Maurice Wohl Clinical Neuroscience Institute, King's College London, London SE5 9NU, United Kingdom.
Seung-Chan KimUK-Dementia Research Institute, Department of Basic and Clinical Neuroscience, Maurice Wohl Clinical Neuroscience Institute, King's College London, London SE5 9NU, United Kingdom.
Younbok LeeUK-Dementia Research Institute, Department of Basic and Clinical Neuroscience, Maurice Wohl Clinical Neuroscience Institute, King's College London, London SE5 9NU, United Kingdom.
Jee Hyun YiHenry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, Bristol Medical School, Faculty of Health Sciences, University of Bristol, Bristol BS1 3NY, United Kingdom.
Saviana A BarbatiUK-Dementia Research Institute, Department of Basic and Clinical Neuroscience, Maurice Wohl Clinical Neuroscience Institute, King's College London, London SE5 9NU, United Kingdom.
Christopher ShawUK-Dementia Research Institute, Department of Basic and Clinical Neuroscience, Maurice Wohl Clinical Neuroscience Institute, King's College London, London SE5 9NU, United Kingdom.
Kwangwook ChoHenry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, Bristol Medical School, Faculty of Health Sciences, University of Bristol, Bristol BS1 3NY, United Kingdom kei.cho@kcl.ac.uk.
UK Dementia Research Institute · GBKing's College London · GBUniversity of Bristol · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 203249/Z/16/Z
6 · The paper itself

Abstract

Hyperphosphorylation of the microtubule associated protein tau (tau) is inextricably linked to several neurodegenerative diseases, collectively termed tauopathies, in which synapse dysfunction occurs through largely unidentified mechanisms. Our research aimed to uncover molecular mechanisms by which phosphorylation of tau (pTau) affects synapse function. Using combined molecular and electrophysiological analysis with in vitro genetic knock-in of phosphorylation mutant human tau in male rat CA1 hippocampal neurons, we show an interplay between tau and protein kinase C and casein kinase substrate in neurons protein 1 (PACSIN1) that regulates synapse function. pTau at serine residues 396/404 decreases tau:PACSIN1 binding and evokes PACSIN1-dependent functional and structural synapse weakening. Knock-down of tau or PACSIN1 increases AMPA receptor (AMPAR)-mediated current at extrasynaptic regions, supporting a role for these proteins in affecting AMPAR trafficking. The pTau-induced PACSIN1 dissociation may represent a pathophysiological regulator of synapse function that underlies tauopathy-associated synapse defects.

Indexed as

Action PotentialsAnimalsCytoskeletal ProteinsExcitatory Postsynaptic PotentialsGene Knockdown TechniquesHEK293 CellsHippocampusHumansMaleMutation, MissenseNerve Tissue ProteinsPatch-Clamp TechniquesPhosphorylationProtein Interaction MappingProtein Processing, Post-TranslationalRatsCytoskeletal ProteinsMapt protein, ratNerve Tissue ProteinsPacsin1 protein, ratReceptors, GlutamateRecombinant ProteinsRNA, Small Interferingtau ProteinsAlzheimer's diseaseAMPA receptorPACSIN1phosphorylationsynapseTau

Identifiers

PMID34290082
PMCPMC8387117
OpenAlexW3185565059

What OpenQuestion holds

Textmetadata
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.