A secretory phospholipase D hydrolyzes phosphatidylcholine to suppress rice heading time.

ABSTRACT: Phospholipase D (PLD) hydrolyzes membrane phospholipids and is crucial in various physiological processes and transduction of different signals. Secretory phospholipases play important roles in mammals, however, whose functions in plants remain largely unknown. We previously identified a rice secretory PLD (spPLD) that harbors a signal peptide and here we reported the secretion and function of spPLD in rice heading time regulation. Subcellular localization analysis confirmed the signal peptide is indispensable for spPLD secretion into the extracellular spaces, where spPLD hydrolyzes substrates. spPLD overexpression results in delayed heading time which is dependent on its secretory character, while suppression or deficiency of spPLD led to the early heading of rice under both short-day and

SUBMITTER: Qu L 

PROVIDER: S-EPMC8654219 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature