Evidence map›Paper›PMID 21998198›Full record

ArticleMolecular biology of the cell2011

The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse.

Jennifer Larimore, Karine Tornieri, Pearl V Ryder, Avanti Gokhale, Stephanie A Zlatic, Branch Craige, Joshua D Lee, Konrad Talbot, Jean-Francois Pare, Yoland Smith and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 68 citations in OpenAlex.

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  3. Two High-QualityInternational journal of molecular sciences · 2023
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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

11 authors at 3 institutions in 1 country.

Jennifer LarimoreDepartment of Cell Biology, Emory University, Atlanta, GA 30322, USA.
Karine Tornieri
Pearl V Ryder
Avanti Gokhale
Stephanie A Zlatic
Branch Craige
Joshua D Lee
Konrad Talbot
Jean-Francois Pare
Yoland Smith
Victor Faundez
Emory University · USEmory National Primate Research CenterUniversity of Pennsylvania · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM008169 · NIGMS · EMORY UNIVERSITY · PI GROSS, ROBERT E · 1987 to 2021
$20.3M
ENNCF - Viral Vector CoreP30NS055077 · NINDS · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2008 to 2018
$6.8M
Cellular Mechanisms of Neuronal Metal Transport and ToxicityR01GM077569 · NIGMS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2006 to 2016
$2.6M
Mechanisms of Endosome Trafficking in NeuronsR01NS042599 · NINDS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2003 to 2012
$2.5M
Mechanisms of Endosome Trafficking in NeuronsR56NS042599 · NINDS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2008 to 2008
$339k
NIGMS NIH HHS GM077569NIGMS NIH HHS R01 GM077569NIGMS NIH HHS T32 GM008169NINDS NIH HHS NS42599NINDS NIH HHS P30 NS055077NINDS NIH HHS P30NS055077NINDS NIH HHS R01 NS042599NINDS NIH HHS R56 NS042599
6 · The paper itself

Abstract

Dysbindin assembles into the biogenesis of lysosome-related organelles complex 1 (BLOC-1), which interacts with the adaptor protein complex 3 (AP-3), mediating a common endosome-trafficking route. Deficiencies in AP-3 and BLOC-1 affect synaptic vesicle composition. However, whether AP-3-BLOC-1-dependent sorting events that control synapse membrane protein content take place in cell bodies upstream of nerve terminals remains unknown. We tested this hypothesis by analyzing the targeting of phosphatidylinositol-4-kinase type II α (PI4KIIα), a membrane protein present in presynaptic and postsynaptic compartments. PI4KIIα copurified with BLOC-1 and AP-3 in neuronal cells. These interactions translated into a decreased PI4KIIα content in the dentate gyrus of dysbindin-null BLOC-1 deficiency and AP-3-null mice. Reduction of PI4KIIα in the dentate reflects a failure to traffic from the cell body. PI4KIIα was targeted to processes in wild-type primary cultured cortical neurons and PC12 cells but failed to reach neurites in cells lacking either AP-3 or BLOC-1. Similarly, disruption of an AP-3-sorting motif in PI4KIIα impaired its sorting into processes of PC12 and primary cultured cortical neuronal cells. Our findings indicate a novel vesicle transport mechanism requiring BLOC-1 and AP-3 complexes for cargo sorting from neuronal cell bodies to neurites and nerve terminals.

Indexed as

Adaptor Protein Complex 3Amino Acid MotifsAnimalsCarrier ProteinsDysbindinDystrophin-Associated ProteinsIntracellular Signaling Peptides and ProteinsLectinsMiceMice, Mutant StrainsNerve Tissue ProteinsNeuritesPC12 CellsRatsSynaptic MembranesTransport VesiclesAdaptor Protein Complex 3Bloc1s6 protein, mouseCarrier ProteinsDtnbp1 protein, mouseDysbindinDystrophin-Associated ProteinsIntracellular Signaling Peptides and ProteinsLectinsNerve Tissue Proteins

Identifiers

PMID21998198
PMCPMC3237628
OpenAlexW2102004133

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.