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A clade of receptor-like cytoplasmic kinases and 14-3-3 proteins coordinate inositol hexaphosphate accumulation. | LitMetric

AI Article Synopsis

  • Inositol hexaphosphate (InsP) is the primary way phosphorus is stored in seeds, and reducing its levels is important for improving animal nutrition and minimizing environmental impact.
  • Researchers identified a group of proteins called Inositol Polyphosphate-related Cytoplasmic Kinases (IPCK1-IPCK6) that play a key role in regulating InsP levels in seeds.
  • In mutant seeds lacking these kinases, InsP levels dropped significantly while phosphate levels increased, suggesting that IPCKs help control InsP synthesis by recruiting specific proteins and forming a complex that enhances InsP biosynthesis.

Article Abstract

Inositol hexaphosphate (InsP) is the major storage form of phosphorus in seeds. Reducing seed InsP content is a breeding objective in agriculture, as InsP negatively impacts animal nutrition and the environment. Nevertheless, how InsP accumulation is regulated remains largely unknown. Here, we identify a clade of receptor-like cytoplasmic kinases (RLCKs), named Inositol Polyphosphate-related Cytoplasmic Kinases 1-6 (IPCK1-IPCK6), deeply involved in InsP accumulation. The InsP concentration is dramatically reduced in seeds of ipck quadruple (T-4m/C-4m) and quintuple (C-5m) mutants, accompanied with the obviously increase of phosphate (Pi) concentration. The plasma membrane-localized IPCKs recruit IPK1 involved in InsP synthesis, and facilitate its binding and activity via phosphorylation of GRF 14-3-3 proteins. IPCKs also recruit IPK2s and PI-PLCs required for InsP/InsP and InsP biosynthesis respectively, to form a potential IPCK-GRF-PLC-IPK2-IPK1 complex. Our findings therefore uncover a regulatory mechanism of InsP accumulation governed by IPCKs, shedding light on the mechanisms of InsP biosynthesis in eukaryotes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11178898PMC
http://dx.doi.org/10.1038/s41467-024-49102-6DOI Listing

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