Evidence map›Paper›PMID 27425610›Full record

ArticleCell reports2016

Synthesis of Isomeric Phosphoubiquitin Chains Reveals that Phosphorylation Controls Deubiquitinase Activity and Specificity.

Nicolas Huguenin-Dezot, Virginia De Cesare, Julien Peltier, Axel Knebel, Yosua Adi Kristaryianto, Daniel T Rogerson, Yogesh Kulathu, Matthias Trost, Jason W Chin

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 69 citations in OpenAlex.

  1. Substrate biasing in UCHL5 proteoforms.bioRxiv : the preprint server for biology · 2026
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  9. Reading and Writing the Ubiquitin Code Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024
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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

9 authors at 4 institutions in 1 country.

Nicolas Huguenin-DezotMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, CB2 OQH Cambridge, UK.
Virginia De CesareMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, DD1 5EH Dundee, UK.
Julien PeltierMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, DD1 5EH Dundee, UK.
Axel KnebelMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, DD1 5EH Dundee, UK.
Yosua Adi KristaryiantoMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, DD1 5EH Dundee, UK.
Daniel T RogersonMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, CB2 OQH Cambridge, UK.
Yogesh KulathuMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, DD1 5EH Dundee, UK.
Matthias TrostMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, DD1 5EH Dundee, UK. Electronic address: m.trost@dundee.ac.uk.
Jason W ChinMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, CB2 OQH Cambridge, UK. Electronic address: chin@mrc-lmb.cam.ac.uk.
Medical Research Council · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GBMRC Laboratory of Molecular Biology · GBUniversity of Dundee · GB

Funding

Medical Research Council MC_U105181009Medical Research Council MC_UP_A024_1008Medical Research Council MC_UP_A500_1020Medical Research Council MC_UU_12016/5Medical Research Council MC_UU_12016/6
6 · The paper itself

Abstract

Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and serine 65 via genetic code expansion. We use these phosphoubiquitins for the enzymatic assembly of 20 isomeric phosphoubiquitin dimers, with different sites of isopeptide linkage and/or phosphorylation. We discover that phosphorylation of serine 20 on ubiquitin converts UBE3C from a dual-specificity E3 ligase into a ligase that primarily synthesizes K48 chains. We profile the activity of 31 deubiquitinases on the isomeric phosphoubiquitin dimers in 837 reactions, and we discover that phosphorylation at distinct sites in ubiquitin can activate or repress cleavage of a particular linkage by deubiquitinases and that phosphorylation at a single site in ubiquitin can control the specificity of deubiquitinases for distinct ubiquitin linkages.

Indexed as

Binding SitesDeubiquitinating EnzymesHumansPhosphorylationSerineUbiquitinUbiquitin-Protein LigasesDeubiquitinating EnzymesSerineUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID27425610
PMCPMC4967478
OpenAlexW2471938860

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.