Evidence map›Paper›PMID 32525583›Full record

ArticleThe EMBO journal2020

CALCOCO1 acts with VAMP-associated proteins to mediate ER-phagy.

Thaddaeus Mutugi Nthiga, Birendra Kumar Shrestha, Eva Sjøttem, Jack-Ansgar Bruun, Kenneth Bowitz Larsen, Zambarlal Bhujabal, Trond Lamark, Terje Johansen

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
12.7field-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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Pooled it
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  12. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
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32 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Thaddaeus Mutugi NthigaDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.
Birendra Kumar ShresthaDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0002-8972-0308
Eva SjøttemDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.
Jack-Ansgar BruunDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0003-0614-2790
Kenneth Bowitz LarsenDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0001-6061-4686
Zambarlal BhujabalDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.
Trond LamarkDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0001-6338-3342
Terje JohansenDepartment of Medical Biology, Molecular Cancer Research Group, University of Tromsø-The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0003-1451-9578
UiT The Arctic University of Norway · NO

Funding

Norges Forskningsråd (Forskningsrådet) 214448Norges Forskningsråd (Forskningsrådet) 249884
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) plays important roles in protein synthesis and folding, and calcium storage. The volume of the ER and expression of its resident proteins are increased in response to nutrient stress. ER-phagy, a selective form of autophagy, is involved in the degradation of the excess components of the ER to restore homeostasis. Six ER-resident proteins have been identified as ER-phagy receptors so far. In this study, we have identified CALCOCO1 as a novel ER-phagy receptor for the degradation of the tubular ER in response to proteotoxic and nutrient stress. CALCOCO1 is a homomeric protein that binds directly to ATG8 proteins via LIR- and UDS-interacting region (UIR) motifs acting co-dependently. CALCOCO1-mediated ER-phagy requires interaction with VAMP-associated proteins VAPA and VAPB on the ER membranes via a conserved FFAT-like motif. Depletion of CALCOCO1 causes expansion of the ER and inefficient basal autophagy flux. Unlike the other ER-phagy receptors, CALCOCO1 is peripherally associated with the ER. Therefore, we define CALCOCO1 as a soluble ER-phagy receptor.

Indexed as

AutophagyAnimalsCalcium-Binding ProteinsEndoplasmic ReticulumHeLa CellsHumansIntracellular MembranesMiceTranscription FactorsVesicular Transport ProteinsCalcium-Binding ProteinsCALCOCO1 protein, humanCalcoco1 protein, mouseTranscription FactorsVAPA protein, humanVapa protein, mouseVAPB protein, humanVAPB protein, mouseVesicular Transport ProteinsAutophagyCALCOCO1ER-phagyFFATVAPA

Identifiers

PMID32525583
PMCPMC7396842
OpenAlexW3033615903

What OpenQuestion holds

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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.