ArticlePLoS genetics2021
A secretory phospholipase D hydrolyzes phosphatidylcholine to suppress rice heading time.
Article in PLoS genetics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Integrative phenomics, metabolomics and genomics analysis provides new insights for deciphering the genetic basis of metabolism in polished rice.Genome biology · 2025Article
- Review
- Phosphorus-Mediated Transition from Vegetative to Reproductive Growth in Dwarf Coconut (International journal of molecular sciences · 2024Article
- Exploring the response of yellow lupine (Lupinus luteus L.) root to drought mediated by pathways related to phytohormones, lipid, and redox homeostasis.BMC plant biology · 2024Article
- The Function of Florigen in the Vegetative-to-Reproductive Phase Transition in and around the Shoot Apical Meristem.Plant & cell physiology · 2024Review
- Environmental control of rice flowering time.Plant communications · 2023Review
- A stress-inducible protein regulates drought tolerance and flowering time in Brachypodium and Arabidopsis.Plant physiology · 2023Article
- An adaptive teosinteProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Characterization and evolutionary diversification of the phospholipase D gene family in mosses.Frontiers in genetics · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 long-day conditions, which is consistent with that spPLD overexpression/suppression indeed led to the reduced/increased Hd3a/RFT1 (Arabidopsis Flowing Locus T homolog) activities. Interestingly, rice Hd3a and RFT1 bind to phosphatidylcholines (PCs) and a further analysis by lipidomic approach using mass spectrometry revealed the altered phospholipids profiles in shoot apical meristem, particularly the PC species, under altered spPLD expressions. These results indicate the significance of secretory spPLD and help to elucidate the regulatory network of rice heading time.
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