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The E3 ubiquitin ligase SINA1 and the protein kinase BIN2 cooperatively regulate PHR1 in apple anthocyanin biosynthesis.

Jian-Ping AnHong-Liang LiZhi-Ying LiuDa-Ru WangChun-Xiang YouYuepeng Han
Published in: Journal of integrative plant biology (2023)
PHR1 (PHOSPHATE STARVATION RESPONSE1) plays key roles in the phosphate (Pi) starvation response and in Pi-deficiency-induced anthocyanin biosynthesis in plants. However, the post-translational regulation of PHR1 is unclear, and the molecular basis of PHR1-mediated anthocyanin biosynthesis remains elusive. In this study, we determined that MdPHR1 was essential for Pi-deficiency-induced anthocyanin accumulation in apple (Malus × domestica). MdPHR1 interacted with MdWRKY75, a positive regulator of anthocyanin biosynthesis, to enhance the MdWRKY75-activated transcription of MdMYB1, leading to anthocyanin accumulation. In addition, the E3 ubiquitin ligase SEVEN IN ABSENTIA1 (MdSINA1) negatively regulated MdPHR1-promoted anthocyanin biosynthesis via the ubiquitination-mediated degradation of MdPHR1. Moreover, the protein kinase MdBIN2 phosphorylated MdPHR1 and positively regulated MdPHR1-mediated anthocyanin accumulation by attenuating the MdSINA1-mediated ubiquitination degradation of MdPHR1. Taken together, these findings not only demonstrate the regulatory role of MdPHR1 in Pi-starvation induced anthocyanin accumulation, but also provide an insight into the post-translational regulation of PHR1. This article is protected by copyright. All rights reserved.
Keyphrases
  • transcription factor
  • protein kinase
  • high glucose
  • diabetic rats
  • cell wall
  • drug induced
  • replacement therapy