Back to Search
Start Over
Root membrane ubiquitinome under short-term osmotic stress
Root membrane ubiquitinome under short-term osmotic stress
- Source :
- International Journal of Molecular Sciences; Volume 23; Issue 4; Pages: 1956
- Publication Year :
- 2021
- Publisher :
- HAL CCSD, 2021.
-
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. Plants use the ubiquitin (Ub) proteasome system to modulate protein content, and a role for Ub in mediating endocytosis and trafficking plant plasma membrane proteins has recently emerged. In this study, we used the K-ε-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 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 putatively in protein internalization as described for the aquaporin PIP2;1. Our in silico analysis of ubiquitinated proteins shows that two E2 Ub ligases, 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.
- Subjects :
- Proteomics
0106 biological sciences
Proteome
[SDV]Life Sciences [q-bio]
Arabidopsis
aquaporin
mass spectrometry
osmotic stress
ubiquitination
Plant Roots
01 natural sciences
Catalysis
Inorganic Chemistry
03 medical and health sciences
Osmotic Pressure
ddc:570
[SDV.BV]Life Sciences [q-bio]/Vegetal Biology
Physical and Theoretical Chemistry
Molecular Biology
Spectroscopy
030304 developmental biology
0303 health sciences
Ubiquitin
Lysine
Organic Chemistry
Membrane Proteins
General Medicine
Ubiquitinated Proteins
Computer Science Applications
Protein Processing, Post-Translational
010606 plant biology & botany
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences; Volume 23; Issue 4; Pages: 1956
- Accession number :
- edsair.doi.dedup.....c56d7b7fc86357e24b9bdf0958e20205