Evidence map›Paper›PMID 26202464›Full record

ArticleMolecular biology of the cell2015

The EHD protein Past1 controls postsynaptic membrane elaboration and synaptic function.

Kate Koles, Emily M Messelaar, Zachary Feiger, Crystal J Yu, C Andrew Frank, Avital A Rodal

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 18 citations in OpenAlex.

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  5. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 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

6 authors at 2 institutions in 1 country.

Kate KolesRosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453.
Emily M MesselaarRosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453.
Zachary FeigerRosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453.
Crystal J YuRosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453.
C Andrew FrankDepartment of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242.
Avital A RodalRosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453 arodal@brandeis.edu.
Brandeis University · USUniversity of Iowa · US

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Cale Whitworth · 2014 to 2026
$13.5M
Activity-dependent regulation of membrane traffic and growth signaling in neuronsDP2NS082127 · NINDS · BRANDEIS UNIVERSITY · PI RODAL, AVITAL ADAH · 2012 to 2012
$2.4M
How Ephexin Signaling Promotes Neuronal StabilityR00NS062738 · NINDS · UNIVERSITY OF IOWA · PI FRANK, CARL ANDREW · 2010 to 2012
$725k
How Ephexin Signaling Promotes Neuronal StabilityK99NS062738 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANK, CARL ANDREW · 2008 to 2009
$171k
NCCDPHP CDC HHS DP2 NS082127NIH HHS P40 OD018537NIH HHS P40OD018537NINDS NIH HHS DP2 NS082127NINDS NIH HHS K99 NS062738NINDS NIH HHS NS062738NINDS NIH HHS R00 NS062738
6 · The paper itself

Abstract

Membranes form elaborate structures that are highly tailored to their specialized cellular functions, yet the mechanisms by which these structures are shaped remain poorly understood. Here, we show that the conserved membrane-remodeling C-terminal Eps15 Homology Domain (EHD) protein Past1 is required for the normal assembly of the subsynaptic muscle membrane reticulum (SSR) at the Drosophila melanogaster larval neuromuscular junction (NMJ). past1 mutants exhibit altered NMJ morphology, decreased synaptic transmission, reduced glutamate receptor levels, and a deficit in synaptic homeostasis. The membrane-remodeling proteins Amphiphysin and Syndapin colocalize with Past1 in distinct SSR subdomains and collapse into Amphiphysin-dependent membrane nodules in the SSR of past1 mutants. Our results suggest a mechanism by which the coordinated actions of multiple lipid-binding proteins lead to the elaboration of increasing layers of the SSR and uncover new roles for an EHD protein at synapses.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCarrier ProteinsDrosophila melanogasterDrosophila ProteinsLarvaNerve Tissue ProteinsNeuromuscular JunctionPresynaptic TerminalsReceptors, GlutamateSynaptic MembranesAdaptor Proteins, Signal TransducingamphiphysinCarrier ProteinsDrosophila ProteinsEHD protein-binding protein 1, DrosophilaNerve Tissue ProteinsReceptors, GlutamateSynd protein, Drosophila

Identifiers

PMID26202464
PMCPMC4569317
OpenAlexW1929284950

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.