Evidence map›Paper›PMID 27072891›Full record

ArticleNeurobiology of disease2016

The polarity protein Par3 regulates APP trafficking and processing through the endocytic adaptor protein Numb.

Miao Sun, Suwaiba Z Asghar, Huaye Zhang

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of disease, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.

  1. Pooled it
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  12. The Endolysosomal System and Proteostasis: From Development to Degeneration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    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

3 authors at 1 institution in 1 country.

Miao SunDepartment of Neuroscience and Cell Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States.
Suwaiba Z AsgharDepartment of Neuroscience and Cell Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States.
Huaye ZhangDepartment of Neuroscience and Cell Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, NJ 08854, United States. Electronic address: huaye.zhang@rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Research Education ComponentP30AG019610 · NIA · SUN HEALTH RESEARCH INSTITUTE · PI GONZALEZ HERNANDEZ, GRACIELA · 2001 to 2020
$32.5M
National Brain and Tissue Resource for Parkinson's Disease and Related DisordersU24NS072026 · NINDS · BANNER SUN HEALTH RESEARCH INSTITUTE · PI BEACH, THOMAS G · 2011 to 2015
$7.8M
Polarity determinants in synaptic stability and plasticityR01NS089578 · NINDS · RBHS-ROBERT WOOD JOHNSON MEDICAL SCHOOL · PI ZHANG, HUAYE · 2015 to 2019
$1.9M
The PAR-6/aPKC Polarity Complex in Synaptic Assembly and FunctionR00NS065183 · NINDS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI ZHANG, HUAYE · 2011 to 2013
$738k
The PAR-6/aPKC Polarity Complex in Synaptic Assembly and FunctionK99NS065183 · NINDS · UNIVERSITY OF VIRGINIA · PI ZHANG, HUAYE · 2009 to 2010
$180k
NIA NIH HHS P30 AG019610NINDS NIH HHS K99 NS065183NINDS NIH HHS R00 NS065183NINDS NIH HHS R01 NS089578NINDS NIH HHS U24 NS072026
6 · The paper itself

Abstract

The processing of amyloid precursor protein (APP) into β-amyloid peptide (Aβ) is a key step in the pathogenesis of Alzheimer's disease (AD), and trafficking dysregulations of APP and its secretases contribute significantly to altered APP processing. Here we show that the cell polarity protein Par3 plays an important role in APP processing and trafficking. We found that the expression of full length Par3 is significantly decreased in AD patients. Overexpression of Par3 promotes non-amyloidogenic APP processing, while depletion of Par3 induces intracellular accumulation of Aβ. We further show that Par3 functions by regulating APP trafficking. Loss of Par3 decreases surface expression of APP by targeting APP to the late endosome/lysosome pathway. Finally, we show that the effects of Par3 are mediated through the endocytic adaptor protein Numb, and Par3 functions by interfering with the interaction between Numb and APP. Together, our studies show a novel role for Par3 in regulating APP processing and trafficking.

Indexed as

Adaptor Proteins, Signal TransducingAlzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesCell Cycle ProteinsEndocytosisEndosomesHumansLysosomesMembrane ProteinsProtein Processing, Post-TranslationalProtein TransportAdaptor Proteins, Signal TransducingAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAPP protein, humanCell Cycle ProteinsMembrane ProteinsPARD3 protein, humanAlzheimer diseaseAmyloid precursor protein (APP)Amyloid-β (Aβ)Cell polarityNumbPar3Trafficking

Identifiers

PMID27072891
PMCPMC4930744
OpenAlexW2322035504

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.