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