Evidence map›Paper›PMID 32898700›Full record

ArticleJournal of proteomics2020

Technical report: Targeted proteomic analysis reveals enrichment of atypical ubiquitin chains in contractile murine tissues.

Tiaan Heunis, Frederic Lamoliatte, José Luis Marín-Rubio, Abeer Dannoura, Matthias Trost

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteomics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

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  13. Frontiers in cellular and infection microbiology · 2022
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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

5 authors at 1 institution in 1 country.

Tiaan HeunisBiosciences Institute, Newcastle University, NE2 4HH Newcastle upon Tyne, United Kingdom.
Frederic LamoliatteBiosciences Institute, Newcastle University, NE2 4HH Newcastle upon Tyne, United Kingdom.
José Luis Marín-RubioBiosciences Institute, Newcastle University, NE2 4HH Newcastle upon Tyne, United Kingdom.
Abeer DannouraBiosciences Institute, Newcastle University, NE2 4HH Newcastle upon Tyne, United Kingdom.
Matthias TrostBiosciences Institute, Newcastle University, NE2 4HH Newcastle upon Tyne, United Kingdom. Electronic address: matthias.trost@ncl.ac.uk.
Newcastle University · GB

Funding

Wellcome TrustWellcome Trust 215542/Z/19/Z
6 · The paper itself

Abstract

Ubiquitylation is an elaborate post-translational modification involved in all biological processes. Its pleotropic effect is driven by the ability to form complex polyubiquitin chain architectures that can influence biological functions. In this study, we optimised sample preparation and chromatographic separation of Ubiquitin peptides for Absolute Quantification by Parallel Reaction Monitoring (Ub-AQUA-PRM). Using this refined Ub-AQUA-PRM assay, we were able to quantify all ubiquitin chain types in 10-min LC-MS/MS runs. We used this method to determine the ubiquitin chain-linkage composition in murine bone marrow-derived macrophages and different mouse tissues. We could show tissue-specific differences in ubiquitin levels in murine tissues, with polyubiquitin chain types contributing a small proportion to the total pool of ubiquitin. Interestingly, we observed enrichment of atypical (K33) ubiquitin chains in heart and muscle. Our approach enabled high-throughput screening of ubiquitin chain-linkage composition in different murine tissues and highlighted a possible role for atypical ubiquitylation in contractile tissues. SIGNIFICANCE: Large knowledge gaps exist in our understanding of ubiquitin chain-linkage composition in mammalian tissues. Defining this in vivo ubiquitin chain-linkage landscape could reveal the functional importance of different ubiquitin chain types in tissues. In this study, we refined the previously described Ub-AQUA-PRM assay to enable quantification of all ubiquitin chain types in a high-throughput manner. Using this assay, we provided new data on the ubiquitin chain-linkage composition in primary murine macrophages and tissues, and revealed an enrichment of atypical ubiquitin chains in contractile tissues. Our approach should thus enable rapid, high-throughput screening of ubiquitin chain-linkage composition in different sample types, as demonstrated in murine primary cells and tissues.

Indexed as

ProteomicsUbiquitinAnimalsChromatography, LiquidMicePolyubiquitinTandem Mass SpectrometryUbiquitinationPolyubiquitinUbiquitinAbsolute quantificationAtypical ubiquitin chain typesMurineParallel reaction monitoringPrimary murine macrophagesTissuesUbiquitin chain-linkage

Identifiers

PMID32898700
PMCPMC7567960
OpenAlexW3083133537

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.