Evidence map›Paper›PMID 37422481›Full record

ArticleNature communications2023

ATPase activity of DFCP1 controls selective autophagy.

Viola Nähse, Camilla Raiborg, Kia Wee Tan, Sissel Mørk, Maria Lyngaas Torgersen, Eva Maria Wenzel, Mireia Nager, Veijo T Salo, Terje Johansen, Elina Ikonen and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.0field-weighted citation impact, top 1% 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

30 citing papers in PubMed, 43 citations in OpenAlex.

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  4. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
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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

12 authors at 4 institutions in 4 countries.

Viola NähseCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway. Viola.Naehse@rr-research.no.ORCID 0000-0002-5479-2483
Camilla RaiborgCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway.ORCID 0000-0002-5406-5403
Kia Wee TanCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway.
Sissel MørkCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway.
Maria Lyngaas TorgersenCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway.
Eva Maria WenzelCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway.
Mireia NagerAutophagy Research Group, Department of Medical Biology, University of Tromsø, The Arctic University of Norway, Tromsø, Norway.
Veijo T SaloDepartment of Anatomy and Stem Cells and Metabolism Research Program, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-6991-2142
Elina IkonenDepartment of Anatomy and Stem Cells and Metabolism Research Program, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID 0000-0001-8382-1135
Kay Oliver SchinkCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway. k.o.schink@medisin.uio.no.ORCID 0000-0002-5903-4059
Harald StenmarkCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Montebello, N-0379, Oslo, Norway. h.a.stenmark@medisin.uio.no.ORCID 0000-0002-1971-4252
Oslo University Hospital · NOUniversity of Helsinki · FIUppsala University · SEUiT The Arctic University of Norway · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular homeostasis is governed by removal of damaged organelles and protein aggregates by selective autophagy mediated by cargo adaptors such as p62/SQSTM1. Autophagosomes can assemble in specialized cup-shaped regions of the endoplasmic reticulum (ER) known as omegasomes, which are characterized by the presence of the ER protein DFCP1/ZFYVE1. The function of DFCP1 is unknown, as are the mechanisms of omegasome formation and constriction. Here, we demonstrate that DFCP1 is an ATPase that is activated by membrane binding and dimerizes in an ATP-dependent fashion. Whereas depletion of DFCP1 has a minor effect on bulk autophagic flux, DFCP1 is required to maintain the autophagic flux of p62 under both fed and starved conditions, and this is dependent on its ability to bind and hydrolyse ATP. While DFCP1 mutants defective in ATP binding or hydrolysis localize to forming omegasomes, these omegasomes fail to constrict properly in a size-dependent manner. Consequently, the release of nascent autophagosomes from large omegasomes is markedly delayed. While knockout of DFCP1 does not affect bulk autophagy, it inhibits selective autophagy, including aggrephagy, mitophagy and micronucleophagy. We conclude that DFCP1 mediates ATPase-driven constriction of large omegasomes to release autophagosomes for selective autophagy.

Indexed as

AutophagyMacroautophagyAdenosine TriphosphatasesAdenosine TriphosphateEndoplasmic ReticulumAdenosine TriphosphatasesAdenosine Triphosphate

Identifiers

PMID37422481
PMCPMC10329651
OpenAlexW4383602884

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.