Functional Conservation of the DDP1-type Inositol Pyrophosphate Phosphohydrolases in Land Plant

Abstract

Inositol pyrophosphates (PP-InsPs) are eukaryote-specific second messengers that regulate diverse cellular processes, including immunity, nutrient sensing, and hormone signaling pathways in plants. These energy-rich messengers exhibit high sensitivity to the cellular phosphate status, suggesting that the synthesis and degradation of PP-InsPs are tightly controlled within the cells. Notably, the molecular basis of PP-InsP hydrolysis in plants remains largely unexplored. In this study, we report the functional characterization of MpDDP1, a diadenosine and diphosphoinositol polyphosphate phosphohydrolase encoded by the genome of the liverwort, <i>Marchantia polymorpha</i>. We show that MpDDP1 functions as a PP-InsP phosphohydrolase in different heterologous organisms. Consistent with this finding, <i>M. polymorpha</i> plants defective in MpDDP1 exhibit elevated levels of 1/3-InsP₇ and 1/3,5-InsP₈, highlighting the contribution of MpDDP1 in regulating PP-InsP homeostasis <i>in planta</i>. Furthermore, our study reveals that MpDDP1 controls thallus development and vegetative reproduction in <i>M. polymorpha</i>. Collectively, this study provides insights into the regulation of specific PP-InsP messengers by DDP1-type phosphohydrolases in land plants.