Evidence map›Paper›PMID 28004827›Full record

ArticleNature communications2016

HS1BP3 negatively regulates autophagy by modulation of phosphatidic acid levels.

Petter Holland, Helene Knævelsrud, Kristiane Søreng, Benan J Mathai, Alf Håkon Lystad, Serhiy Pankiv, Gunnveig T Bjørndal, Sebastian W Schultz, Viola H Lobert, Robin B Chan and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

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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 5 institutions in 3 countries.

Petter HollandDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Helene KnævelsrudDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Kristiane SørengDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Benan J MathaiDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Alf Håkon LystadDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Serhiy PankivDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Gunnveig T BjørndalDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.
Sebastian W SchultzCentre for Cancer Biomedicine, Faculty of Medicine and Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, 0379 Oslo, Norway.
Viola H LobertCentre for Cancer Biomedicine, Faculty of Medicine and Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, 0379 Oslo, Norway.
Robin B ChanDepartment of Pathology and Cell Biology, Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Medical Center, 630 West 168th Street, New York, New York 10032, USA.
Bowen ZhouDepartment of Pathology and Cell Biology, Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Medical Center, 630 West 168th Street, New York, New York 10032, USA.
Knut LiestølCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, 0379 Oslo, Norway.
Sven R Carlsson
Thomas J MeliaDepartment of Cell Biology, Yale University School of Medicine, PO Box 208002, 333 Cedar Street, New Haven, Connecticut 06520-800210032, USA.
Gilbert Di PaoloDepartment of Pathology and Cell Biology, Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Medical Center, 630 West 168th Street, New York, New York 10032, USA.
Anne SimonsenDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, PO Box 1112, 0317 Oslo, Norway.ORCID http://orcid.org/0000-0003-4711-7057
University of Oslo · NOColumbia University Irving Medical Center · USOslo University Hospital · NOUmeå University · SEYale University · US

Funding

Regulation of Autophagosome Membrane Dynamics by the AtgB Family of ProteinsR01GM100930 · NIGMS · YALE UNIVERSITY · PI MELIA, THOMAS JAMES · 2013 to 2024
$5.4M
Role of phospholipids in membrane traffic at the synapseR01NS056049 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI LIEM, RONALD K. · 2006 to 2016
$3.7M
Control of liver autophagy by phosphatidic acid signalingR21AG045020 · NIA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI DI PAOLO, GILBERT · 2013 to 2014
$440k
NIA NIH HHS R21 AG045020NIGMS NIH HHS R01 GM100930NINDS NIH HHS R01 NS056049
6 · The paper itself

Abstract

A fundamental question is how autophagosome formation is regulated. Here we show that the PX domain protein HS1BP3 is a negative regulator of autophagosome formation. HS1BP3 depletion increased the formation of LC3-positive autophagosomes and degradation of cargo both in human cell culture and in zebrafish. HS1BP3 is localized to ATG16L1- and ATG9-positive autophagosome precursors and we show that HS1BP3 binds phosphatidic acid (PA) through its PX domain. Furthermore, we find the total PA content of cells to be significantly upregulated in the absence of HS1BP3, as a result of increased activity of the PA-producing enzyme phospholipase D (PLD) and increased localization of PLD1 to ATG16L1-positive membranes. We propose that HS1BP3 regulates autophagy by modulating the PA content of the ATG16L1-positive autophagosome precursor membranes through PLD1 activity and localization. Our findings provide key insights into how autophagosome formation is regulated by a novel negative-feedback mechanism on membrane lipids.

Indexed as

AnimalsAnimals, Genetically ModifiedAutophagosomesAutophagyAutophagy-Related ProteinsCell LineCortactinHEK293 CellsHeLa CellsHumansMembrane LipidsModels, BiologicalNerve Tissue ProteinsPhosphatidic AcidsPhospholipase DProtein DomainsATG16L1 protein, humanAutophagy-Related ProteinsCortactinCTTN protein, humanHS1BP3 protein, humanMembrane LipidsNerve Tissue ProteinsPhosphatidic AcidsPhospholipase Dphospholipase D1Zebrafish Proteins

Identifiers

PMID28004827
PMCPMC5412012
OpenAlexW2566416357

What OpenQuestion holds

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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.