Evidence map›Paper›PMID 29066714›Full record

ArticleNature communications2017

Functional reconstruction of a eukaryotic-like E1/E2/(RING) E3 ubiquitylation cascade from an uncultured archaeon.

Rory Hennell James, Eva F Caceres, Alex Escasinas, Haya Alhasan, Julie A Howard, Michael J Deery, Thijs J G Ettema, Nicholas P Robinson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

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  17. Archaea and the origin of eukaryotes.Nature reviews. Microbiology · 2017
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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

8 authors at 3 institutions in 2 countries.

Rory Hennell JamesDepartment of Biochemistry, The University of Cambridge, Cambridge, CB2 1GA, UK.
Eva F CaceresDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, Uppsala, 751 24, Sweden.
Alex EscasinasDivision of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster, LA1 4YG, UK.
Haya AlhasanDivision of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster, LA1 4YG, UK.
Julie A HowardDepartment of Biochemistry and Cambridge Systems Biology Centre, Cambridge Centre for Proteomics, The University of Cambridge, Cambridge, CB2 1GA, UK.
Michael J DeeryDepartment of Biochemistry and Cambridge Systems Biology Centre, Cambridge Centre for Proteomics, The University of Cambridge, Cambridge, CB2 1GA, UK.
Thijs J G EttemaDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, Uppsala, 751 24, Sweden.ORCID http://orcid.org/0000-0002-6898-6377
Nicholas P RobinsonDivision of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster, LA1 4YG, UK. n.robinson2@lancaster.ac.uk.ORCID http://orcid.org/0000-0002-6094-1924
Lancaster University · GBUniversity of Cambridge · GBUppsala University · SE

Funding

European Research Council 310039
6 · The paper itself

Abstract

The covalent modification of protein substrates by ubiquitin regulates a diverse range of critical biological functions. Although it has been established that ubiquitin-like modifiers evolved from prokaryotic sulphur transfer proteins it is less clear how complex eukaryotic ubiquitylation system arose and diversified from these prokaryotic antecedents. The discovery of ubiquitin, E1-like, E2-like and small-RING finger (srfp) protein components in the Aigarchaeota and the Asgard archaea superphyla has provided a substantive step toward addressing this evolutionary question. Encoded in operons, these components are likely representative of the progenitor apparatus that founded the modern eukaryotic ubiquitin modification systems. Here we report that these proteins from the archaeon Candidatus 'Caldiarchaeum subterraneum' operate together as a bona fide ubiquitin modification system, mediating a sequential ubiquitylation cascade reminiscent of the eukaryotic process. Our observations support the hypothesis that complex eukaryotic ubiquitylation signalling pathways have developed from compact systems originally inherited from an archaeal ancestor.

Indexed as

UbiquitinationArchaeaEukaryotic CellsHumansModels, MolecularMultigene FamilyOperonPhylogenyProteasome Endopeptidase ComplexProtein DomainsSaccharomyces cerevisiaeSignal TransductionSpecies SpecificitySulfurUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesProteasome Endopeptidase ComplexSulfurUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID29066714
PMCPMC5654768
OpenAlexW2750714651

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.