Evidence map›Paper›PMID 28779096›Full record

ArticleScientific reports2017

Quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis.

Nicholas Johnson, Jana Březinová, Elaine Stephens, Emma Burbridge, Matthew Freeman, Colin Adrain, Kvido Strisovsky

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 53 citations in OpenAlex.

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  11. The collectrin-like part of the SARS-CoV-1 and -2 receptor ACE2 is shed by the metalloproteinases ADAM10 and ADAM17.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
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  12. Review
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  17. Interleukin-11 (IL-11) receptor cleavage by the rhomboid protease RHBDL2 induces IL-11 trans-signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
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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

7 authors at 4 institutions in 3 countries.

Nicholas JohnsonInstitute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n. 2, Prague, 166 10, Czech Republic.
Jana BřezinováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n. 2, Prague, 166 10, Czech Republic.ORCID 0000-0002-2076-9891
Elaine StephensMRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom.
Emma BurbridgeInstituto Gulbenkian de Ciência, Lisbon, Portugal.
Matthew FreemanMRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom.
Colin AdrainInstituto Gulbenkian de Ciência, Lisbon, Portugal. cadrain@igc.gulbenkian.pt.
Kvido StrisovskyInstitute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n. 2, Prague, 166 10, Czech Republic. kvido.strisovsky@uochb.cas.cz.
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZInstituto Gulbenkian de Ciência · PTMRC Laboratory of Molecular Biology · GBCharles University · CZ

Funding

Medical Research Council MC_U105178780Wellcome TrustWorldwide Cancer Research 14-1289
6 · The paper itself

Abstract

Rhomboids are intramembrane serine proteases conserved in all kingdoms of life. They regulate epidermal growth factor receptor signalling in Drosophila by releasing signalling ligands from their transmembrane tethers. Their functions in mammals are poorly understood, in part because of the lack of endogenous substrates identified thus far. We used a quantitative proteomics approach to investigate the substrate repertoire of rhomboid protease RHBDL2 in human cells. We reveal a range of novel substrates that are specifically cleaved by RHBDL2, including the interleukin-6 receptor (IL6R), cell surface protease inhibitor Spint-1, the collagen receptor tyrosine kinase DDR1, N-Cadherin, CLCP1/DCBLD2, KIRREL, BCAM and others. We further demonstrate that these substrates can be shed by endogenously expressed RHBDL2 and that a subset of them is resistant to shedding by cell surface metalloproteases. The expression profiles and identity of the substrates implicate RHBDL2 in physiological or pathological processes affecting epithelial homeostasis.

Indexed as

HomeostasisProteomeProteomicsADAM10 ProteinADAM17 ProteinAmino Acid SequenceBinding SitesEpithelial CellsEpitheliumHumansMembrane ProteinsProtein BindingProtein Interaction Domains and MotifsProteolysisSerine EndopeptidasesSerine ProteasesADAM10 ProteinADAM17 ProteinMembrane ProteinsProteomeRHBDL2 protein, humanSerine EndopeptidasesSerine Proteases

Identifiers

PMID28779096
PMCPMC5544772
OpenAlexW2741610891

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.