Evidence map›Paper›PMID 32152276›Full record

ArticleNature communications2020

Endophilin-A coordinates priming and fusion of neurosecretory vesicles via intersectin.

Sindhuja Gowrisankaran, Sébastien Houy, Johanna G Peña Del Castillo, Vicky Steubler, Monika Gelker, Jana Kroll, Paulo S Pinheiro, Dirk Schwitters, Nils Halbsgut, Arndt Pechstein and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

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  13. Organization of Presynaptic Autophagy-Related Processes.Frontiers in synaptic neuroscience · 2022
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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

16 authors at 4 institutions in 4 countries.

Sindhuja GowrisankaranEuropean Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.
Sébastien Houy *University of Copenhagen, Department for Neuroscience, Faculty of Health and Medical Sciences, Copenhagen, Denmark.ORCID http://orcid.org/0000-0003-3639-1931
Johanna G Peña Del Castillo *European Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.
Vicky Steubler *European Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.
Monika GelkerEuropean Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.ORCID http://orcid.org/0000-0002-4001-2730
Jana KrollEuropean Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.ORCID http://orcid.org/0000-0003-4243-4088
Paulo S PinheiroUniversity of Copenhagen, Department for Neuroscience, Faculty of Health and Medical Sciences, Copenhagen, Denmark.
Dirk SchwittersEuropean Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.
Nils HalbsgutEuropean Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany.
Arndt PechsteinLeibniz Research Institute for Molecular Pharmacology, Molecular Physiology and Cell Biology Section, Berlin, Germany.
Jan R T van WeeringDepartment of Clinical Genetics, Center for Neurogenomics and Cognitive Research, Amsterdam UMC, Amsterdam, The Netherlands.
Tanja MaritzenLeibniz Research Institute for Molecular Pharmacology, Molecular Physiology and Cell Biology Section, Berlin, Germany.ORCID http://orcid.org/0000-0003-4993-0340
Volker HauckeLeibniz Research Institute for Molecular Pharmacology, Molecular Physiology and Cell Biology Section, Berlin, Germany.ORCID http://orcid.org/0000-0003-3119-6993
Nuno RaimundoInstitute for Cellular Biochemistry, University Medical Center Göttingen (UMG), Göttingen, Germany.ORCID http://orcid.org/0000-0002-5988-9129
Jakob B SørensenUniversity of Copenhagen, Department for Neuroscience, Faculty of Health and Medical Sciences, Copenhagen, Denmark. jakobbs@sund.ku.dk.ORCID http://orcid.org/0000-0001-5465-3769
Ira MilosevicEuropean Neuroscience Institute-A Joint Initiative of the University Medical Center Göttingen and the Max Planck Society Göttingen, Göttingen, Germany. imilose@gwdg.de.ORCID http://orcid.org/0000-0001-6440-3763
Universitätsmedizin Göttingen · DELeibniz Association · DEUniversity of Copenhagen · DKAmsterdam Neuroscience · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endophilins-A are conserved endocytic adaptors with membrane curvature-sensing and -inducing properties. We show here that, independently of their role in endocytosis, endophilin-A1 and endophilin-A2 regulate exocytosis of neurosecretory vesicles. The number and distribution of neurosecretory vesicles were not changed in chromaffin cells lacking endophilin-A, yet fast capacitance and amperometry measurements revealed reduced exocytosis, smaller vesicle pools and altered fusion kinetics. The levels and distributions of the main exocytic and endocytic factors were unchanged, and slow compensatory endocytosis was not robustly affected. Endophilin-A's role in exocytosis is mediated through its SH3-domain, specifically via a direct interaction with intersectin-1, a coordinator of exocytic and endocytic traffic. Endophilin-A not able to bind intersectin-1, and intersectin-1 not able to bind endophilin-A, resulted in similar exocytic defects in chromaffin cells. Altogether, we report that two endocytic proteins, endophilin-A and intersectin-1, are enriched on neurosecretory vesicles and regulate exocytosis by coordinating neurosecretory vesicle priming and fusion.

Indexed as

AcyltransferasesAdaptor Proteins, Vesicular TransportAnimalsChromaffin CellsCytoplasmic VesiclesDisease Models, AnimalEndocytosisFemaleHumansMaleMiceMice, Inbred C57BLMice, KnockoutNeurosecretory Systems2-acylglycerophosphate acyltransferaseAcyltransferasesAdaptor Proteins, Vesicular Transportintersectin 1

Identifiers

PMID32152276
PMCPMC7062783
OpenAlexW3010205798

What OpenQuestion holds

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Registered trials

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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.