Evidence map›Paper›PMID 35216074›Full record

ArticleInternational journal of molecular sciences2022

Root Membrane Ubiquitinome under Short-Term Osmotic Stress.

Nathalie Berger, Vincent Demolombe, Sonia Hem, Valérie Rofidal, Laura Steinmann, Gabriel Krouk, Amandine Crabos, Philippe Nacry, Lionel Verdoucq, Véronique Santoni

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 20 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

10 authors at 1 institution in 2 countries.

Nathalie BergerBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Vincent DemolombeBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Sonia HemBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Valérie RofidalBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Laura SteinmannBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.ORCID 0000-0002-9992-550X
Gabriel KroukBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Amandine CrabosBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Philippe NacryBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.ORCID 0000-0001-7766-4989
Lionel VerdoucqBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Véronique SantoniBPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.
Centre National de la Recherche Scientifique · FR

Funding

Institut national de la recherche pour l'agriculture, l'alimentation et l'environnement no number
6 · The paper itself

Abstract

Osmotic stress can be detrimental to plants, whose survival relies heavily on proteomic plasticity. Protein ubiquitination is a central post-translational modification in osmotic-mediated stress. In this study, we used the K-Ɛ-GG antibody enrichment method integrated with high-resolution mass spectrometry to compile a list of 719 ubiquitinated lysine (K-Ub) residues from 450 Arabidopsis root membrane proteins (58% of which are transmembrane proteins), thereby adding to the database of ubiquitinated substrates in plants. Although no ubiquitin (Ub) motifs could be identified, the presence of acidic residues close to K-Ub was revealed. Our ubiquitinome analysis pointed to a broad role of ubiquitination in the internalization and sorting of cargo proteins. Moreover, the simultaneous proteome and ubiquitinome quantification showed that ubiquitination is mostly not involved in membrane protein degradation in response to short osmotic treatment but that it is putatively involved in protein internalization, as described for the aquaporin PIP2;1. Our in silico analysis of ubiquitinated proteins shows that two E2 Ub-conjugating enzymes, UBC32 and UBC34, putatively target membrane proteins under osmotic stress. Finally, we revealed a positive role for UBC32 and UBC34 in primary root growth under osmotic stress.

Indexed as

ArabidopsisLysineMembrane ProteinsOsmotic PressurePlant RootsProtein Processing, Post-TranslationalProteomeProteomicsUbiquitinUbiquitinated ProteinsUbiquitinationLysineMembrane ProteinsProteomeUbiquitinUbiquitinated Proteinsaquaporinmass spectrometryosmotic stressubiquitination

Identifiers

PMID35216074
PMCPMC8879470
OpenAlexW4221068470

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.