TY  - JOUR
A1  - Berger, Nathalie
A1  - Demolombe, Vincent
A1  - Hem, Sonia
A1  - Rofidal, Valérie
A1  - Steinmann, Laura
A1  - Krouk, Gabriel
A1  - Crabos, Amandine
A1  - Nacry, Philippe
A1  - Verdoucq, Lionel
A1  - Santoni, Véronique
T1  - Root membrane ubiquitinome under short-term osmotic stress
JF  - International Journal of Molecular Sciences
N2  - 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.
KW  - aquaporin
KW  - mass spectrometry
KW  - osmotic stress
KW  - ubiquitination
Y1  - 2022
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-284003
SN  - 1422-0067
VL  - 23
IS  - 4
ER  -