<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Berger N</submitter><funding>Institut national de la recherche pour l'agriculture, l'alimentation et l'environnement</funding><funding>Institut national de la recherche pour l&amp;apos;agriculture, l&amp;apos;alimentation et l&amp;apos;environnement</funding><pagination>1956</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8879470</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(4)</volume><pubmed_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 a</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Root Membrane Ubiquitinome under Short-Term Osmotic Stress.</pubmed_title><pmcid>PMC8879470</pmcid><funding_grant_id>no number</funding_grant_id><pubmed_authors>Rofidal V</pubmed_authors><pubmed_authors>Crabos A</pubmed_authors><pubmed_authors>Nacry P</pubmed_authors><pubmed_authors>Berger N</pubmed_authors><pubmed_authors>Hem S</pubmed_authors><pubmed_authors>Demolombe V</pubmed_authors><pubmed_authors>Steinmann L</pubmed_authors><pubmed_authors>Krouk G</pubmed_authors><pubmed_authors>Verdoucq L</pubmed_authors><pubmed_authors>Santoni V</pubmed_authors></additional><is_claimable>false</is_claimable><name>Root Membrane Ubiquitinome under Short-Term Osmotic Stress.</name><description>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 a</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Feb</publication><modification>2026-04-08T17:53:34.585Z</modification><creation>2025-02-19T05:04:54.156Z</creation></dates><accession>S-EPMC8879470</accession><cross_references><pubmed>35216074</pubmed><doi>10.3390/ijms23041956</doi></cross_references></HashMap>