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Protein phosphorylation is an important post-translational modification that can regulate the protein function. The current knowledge on the phosphorylation status of plant oil body (OB) proteins is inadequate. This present study identifies the distinct physiological substrates of  Arabidopsis  serine/threonine/tyrosine protein kinase  ( STYK) and its role in seed oil accumulation; the role of  Arabidopsis  OLE1, a major seed OB protein has also been elucidated.  In vitro  kinase assay followed by mass spectrometry identifies residue that are phosphorylated by STYK. Further, co-expression of OLE1 and STYK in yeast cells increases the cellular lipid levels and reduces the total lipid when OLE1 was replaced with OLE1 T166A . Moreover, i n vivo  experiments with OB isolated from wild-type and  styk  knock-out lines show the ability of STYK to phosphorylate distinct OB proteins. OLE1 T166A  mutant and  Arabidopsis styk  mutant demonstrate the significant reduction of its substrate phosphorylation.  styk  mutant line significantly reduces the amount of total seed oil as compared to wild-type seeds. Together, our results provide the evidences that Arabidopsis At2G24360 (STYK) is phosphorylating oil body proteins and the phosphorylation regulates the oil content in Arabidopsis seeds.

Arabidopsis serine/threonine/tyrosine protein kinase phosphorylates oil body proteins that regulate oil content in the seeds