UBIQUITIN-CONJUGATING ENZYME34 mediates pyrophosphatase AVP1 turnover and regulates abiotic stress responses in Arabidopsis.

ABSTRACT: Understanding the molecular mechanisms of abiotic stress responses in plants is instrumental for the development of climate-resilient crops. Key factors in abiotic stress responses, such as the proton-pumping pyrophosphatase (AVP1), have been identified, but their function and regulation remain elusive. Here, we explored the post-translational regulation of AVP1 by the ubiquitin-conjugating enzyme UBC34 and its relevance in the salt stress and phosphate starvation responses of Arabidopsis (Arabidopsis thaliana). Through in vitro and in vivo assays, we established that UBC34 interacts with and ubiquitylates AVP1. Mutant lines in which UBC34 was downregulated showed higher tolerance to salt and low inorganic phosphate (Pi) stresses, while we observed the opposite for plants overexpressing UB

SUBMITTER: Xu Q 

PROVIDER: S-EPMC11809586 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature