Evidence map›Paper›PMID 36078095›Full record

ArticleCells2022

Tetraspanin 8 Subfamily Members Regulate Substrate-Specificity of a Disintegrin and Metalloprotease 17.

Miryam Müller, Claire Saunders, Anke Senftleben, Johannes P W Heidbuechel, Birgit Halwachs, Julia Bolik, Nina Hedemann, Christian Röder, Dirk Bauerschlag, Stefan Rose-John and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

7 citing papers in PubMed, 13 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

11 authors at 3 institutions in 2 countries.

Miryam MüllerInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.ORCID 0000-0002-0751-1407
Claire SaundersInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.
Anke SenftlebenInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.
Johannes P W HeidbuechelInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.
Birgit HalwachsTumour Immunology Laboratory, Department of Biosciences and Medical Biology, Paris-Lodron-University Salzburg, 5020 Salzburg, Austria.
Julia BolikInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.
Nina HedemannDepartment of Gynaecology, University Medical Center Schleswig-Holstein, 24105 Kiel, Germany.
Christian RöderInstitute of Experimental Cancer Research, Medical Faculty, University Medical Center Schleswig-Holstein, 24105 Kiel, Germany.
Dirk BauerschlagDepartment of Gynaecology, University Medical Center Schleswig-Holstein, 24105 Kiel, Germany.
Stefan Rose-JohnInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.ORCID 0000-0002-7519-3279
Dirk Schmidt-ArrasInstitute of Biochemistry, Medical Faculty, Christian-Albrechts-University Kiel, 24118 Kiel, Germany.ORCID 0000-0002-1072-7495
Christian-Albrechts-Universität zu Kiel · DEUniversity Hospital Schleswig-Holstein · DEUniversity of Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ectodomain shedding is an irreversible process to regulate inter- and intracellular signaling. Members of the a disintegrin and metalloprotease (ADAM) family are major mediators of ectodomain shedding. ADAM17 is involved in the processing of multiple substrates including tumor necrosis factor (TNF) α and EGF receptor ligands. Substrates of ADAM17 are selectively processed depending on stimulus and cellular context. However, it still remains largely elusive how substrate selectivity of ADAM17 is regulated. Tetraspanins (Tspan) are multi-membrane-passing proteins that are involved in the organization of plasma membrane micro-domains and diverse biological processes. Closely related members of the Tspan8 subfamily, including CD9, CD81 and Tspan8, are associated with cancer and metastasis. Here, we show that Tspan8 subfamily members use different strategies to regulate ADAM17 substrate selectivity. We demonstrate that in particular Tspan8 associates with both ADAM17 and TNF α and promotes ADAM17-mediated TNF α release through recruitment of ADAM17 into Tspan-enriched micro-domains. Yet, processing of other ADAM17 substrates is not altered by Tspan8. We, therefore, propose that Tspan8 contributes to tumorigenesis through enhanced ADAM17-mediated TNF α release and a resulting increase in tissue inflammation.

Indexed as

ADAM ProteinsDisintegrinsMembrane ProteinsSubstrate SpecificityTetraspaninsTumor Necrosis Factor-alphaADAM ProteinsDisintegrinsMembrane ProteinsTetraspaninsTumor Necrosis Factor-alphainflammationproteasestetraspaninTNF

Identifiers

PMID36078095
PMCPMC9454446
OpenAlexW4293527732

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.