Integrated proteomic analysis reveals interactions between phosphorylation and ubiquitination in rose response to Botrytis infection.

ABSTRACT: As two of the most abundant post-translational modifications, phosphorylation and ubiquitination play a significant role in modulating plant-pathogen interactions and increasing evidence indicates their crosstalk in plant immunity. Rose (Rosa sp.) is one of the most important ornamental plants and can be seriously infected by Botrytis cinerea. Here, integrated proteomics analysis was performed to detect global proteome, phosphorylation, and ubiquitination changes in rose upon B. cinerea infection and investigate the possible phosphorylation and ubiquitination crosstalk. A total of 6165 proteins, 11 774 phosphorylation and 10 582 ubiquitination sites, and 77 phosphorylation and 13 ubiquitination motifs were identified. Botrytis cinerea infection resulted in 169 u

SUBMITTER: Li R 

PROVIDER: S-EPMC10782497 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature