Evidence map›Paper›PMID 30258054›Full record

ArticleNature communications2018

A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes.

Martina Foglizzo, Adam J Middleton, Abigail E Burgess, Jennifer M Crowther, Renwick C J Dobson, James M Murphy, Catherine L Day, Peter D Mace

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 40 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

8 authors at 4 institutions in 3 countries.

Martina FoglizzoBiochemistry Department, School of Biomedical Sciences, University of Otago, P.O. Box 56, 710, Cumberland St., Dunedin, 9054, New Zealand.ORCID http://orcid.org/0000-0001-9132-4737
Adam J MiddletonBiochemistry Department, School of Biomedical Sciences, University of Otago, P.O. Box 56, 710, Cumberland St., Dunedin, 9054, New Zealand.ORCID http://orcid.org/0000-0002-6075-4061
Abigail E BurgessBiochemistry Department, School of Biomedical Sciences, University of Otago, P.O. Box 56, 710, Cumberland St., Dunedin, 9054, New Zealand.ORCID http://orcid.org/0000-0002-3522-6347
Jennifer M CrowtherBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch, 8140, New Zealand.ORCID http://orcid.org/0000-0002-9670-2204
Renwick C J DobsonBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch, 8140, New Zealand.ORCID http://orcid.org/0000-0002-5506-4939
James M MurphyThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.ORCID http://orcid.org/0000-0003-0195-3949
Catherine L DayBiochemistry Department, School of Biomedical Sciences, University of Otago, P.O. Box 56, 710, Cumberland St., Dunedin, 9054, New Zealand.ORCID http://orcid.org/0000-0003-1571-4367
Peter D MaceBiochemistry Department, School of Biomedical Sciences, University of Otago, P.O. Box 56, 710, Cumberland St., Dunedin, 9054, New Zealand. peter.mace@otago.ac.nz.ORCID http://orcid.org/0000-0003-2175-9537
University of Otago · NZBiotechnology Institute · USThe University of Melbourne · AUUniversity of Canterbury · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Attachment of ubiquitin to lysine 119 of Histone 2A (H2AK119Ub) is an epigenetic mark characteristic of repressed developmental genes, which is removed by the Polycomb Repressive-Deubiquitinase (PR-DUB) complex. Here we report the crystal structure of the Drosophila PR-DUB, revealing that the deubiquitinase Calypso and its activating partner ASX form a 2:2 complex. The bidentate Calypso-ASX complex is generated by dimerisation of two activated Calypso proteins through their coiled-coil regions. Disrupting the Calypso dimer interface does not affect inherent catalytic activity, but inhibits removal of H2AK119Ub as a consequence of impaired recruitment to nucleosomes. Mutating the equivalent surface on the human counterpart, BAP1, also compromises activity on nucleosomes. Together, this suggests that high local concentrations drive assembly of bidentate PR-DUB complexes on chromatin-providing a mechanistic basis for enhanced PR-DUB activity at specific genomic foci, and the impact of distinct classes of PR-DUB mutations in tumorigenesis.

Indexed as

AnimalsDeubiquitinating EnzymesDrosophilaHumansMolecular StructureMutation, MissenseNucleosomesPolycomb-Group ProteinsDeubiquitinating EnzymesNucleosomesPolycomb-Group Proteins

Identifiers

PMID30258054
PMCPMC6158172
OpenAlexW2889826946

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.