Root membrane ubiquitinome under short-term osmotic stress
Zitieren Sie bitte immer diese URN: urn:nbn:de:bvb:20-opus-284003
- 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 ubiquitinOsmotic 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.…
Autor(en): | Nathalie Berger, Vincent Demolombe, Sonia Hem, Valérie Rofidal, Laura Steinmann, Gabriel Krouk, Amandine Crabos, Philippe Nacry, Lionel Verdoucq, Véronique Santoni |
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URN: | urn:nbn:de:bvb:20-opus-284003 |
Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
Institute der Universität: | Fakultät für Biologie / Center for Computational and Theoretical Biology |
Sprache der Veröffentlichung: | Englisch |
Titel des übergeordneten Werkes / der Zeitschrift (Englisch): | International Journal of Molecular Sciences |
ISSN: | 1422-0067 |
Erscheinungsjahr: | 2022 |
Band / Jahrgang: | 23 |
Heft / Ausgabe: | 4 |
Aufsatznummer: | 1956 |
Originalveröffentlichung / Quelle: | International Journal of Molecular Sciences (2022) 23:4, 1956. https://doi.org/10.3390/ijms23041956 |
DOI: | https://doi.org/10.3390/ijms23041956 |
Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Freie Schlagwort(e): | aquaporin; mass spectrometry; osmotic stress; ubiquitination |
Datum der Freischaltung: | 14.07.2023 |
Datum der Erstveröffentlichung: | 10.02.2022 |
Lizenz (Deutsch): | ![]() |