Evidence map›Paper›PMID 38696649›Full record

ArticleG3 (Bethesda, Md.)2024

CED-6/GULP and components of the clathrin-mediated endocytosis machinery act redundantly to correctly display CED-1 on the cell membrane in Caenorhabditis elegans.

Rikke Hindsgaul Harders, Tine H Morthorst, Line E Landgrebe, Anna D Lande, Marie Sikjær Fuglsang, Stine Bothilde Mortensen, Verónica Feteira-Montero, Helene Halkjær Jensen, Jonas Bruhn Wesseltoft, Anders Olsen

Abstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Rikke Hindsgaul HardersDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, Aalborg, DK-9220, Denmark.
Tine H MorthorstDepartment of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, Aarhus, DK-8000, Denmark.
Line E LandgrebeDepartment of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, Aarhus, DK-8000, Denmark.
Anna D LandeDepartment of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, Aarhus, DK-8000, Denmark.
Marie Sikjær FuglsangDepartment of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, Aarhus, DK-8000, Denmark.
Stine Bothilde MortensenDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, Aalborg, DK-9220, Denmark.
Verónica Feteira-MonteroDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, Aalborg, DK-9220, Denmark.
Helene Halkjær JensenDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, Aalborg, DK-9220, Denmark.ORCID 0000-0002-8426-9802
Jonas Bruhn WesseltoftDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, Aalborg, DK-9220, Denmark.
Anders OlsenDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, Aalborg, DK-9220, Denmark.ORCID 0000-0002-9613-9722

Funding

Interdisciplinary Research Consortium in GeroscienceUL1RR024917 · NCRR · BUCK INSTITUTE FOR RESEARCH ON AGING · PI LITHGOW, GORDON J. · 2007 to 2007
$605k
GSSTKaren Elise Jensen's FoundationNCRR NIH HHS UL1 RR024917NIHNovo Nordic Foundation NNF18OC 0053254
6 · The paper itself

Abstract

CED-1 (cell death abnormal) is a transmembrane receptor involved in the recognition of "eat-me" signals displayed on the surface of apoptotic cells and thus central for the subsequent engulfment of the cell corpse in Caenorhabditis elegans. The roles of CED-1 in engulfment are well established, as are its downstream effectors. The latter include the adapter protein CED-6/GULP and the ATP-binding cassette family homolog CED-7. However, how CED-1 is maintained on the plasma membrane in the absence of engulfment is currently unknown. Here, we show that CED-6 and CED-7 have a novel role in maintaining CED-1 correctly on the plasma membrane. We propose that the underlying mechanism is via endocytosis as CED-6 and CED-7 act redundantly with clathrin and its adaptor, the Adaptor protein 2 complex, in ensuring correct CED-1 localization. In conclusion, CED-6 and CED-7 impact other cellular processes than engulfment of apoptotic cells.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsCell MembraneClathrinEndocytosisAdaptor Protein Complex 2AnimalsApoptosisApoptosis Regulatory ProteinsATP-Binding Cassette TransportersMembrane ProteinsProtein TransportAdaptor Protein Complex 2Apoptosis Regulatory ProteinsATP-Binding Cassette TransportersCaenorhabditis elegans Proteinsced-1 protein, C elegansCED-6 protein, C elegansCED-7 protein, C elegansClathrinMembrane ProteinsAP2Caenorhabditis elegansCED-1CED-6/GULPclathrinCMEdyneinendocytosis

Identifiers

PMID38696649
PMCPMC11228867

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.