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AGC kinases OXI1 and AGC2-2 regulate camalexin secretion and disease resistance by phosphorylating transporter PDR6.
Han, Juan; Liu, Chang-Xin; Liu, Jian; Wang, Cheng-Run; Wang, Shun-Chang; Miao, Guopeng.
Afiliação
  • Han J; Department of Bioengineering, Huainan Normal University, Huainan, Anhui Province 232038, China.
  • Liu CX; Institute of Digital Ecology and Health, Huainan Normal University, Huainan, Anhui Province 232038, China.
  • Liu J; Department of Bioengineering, Huainan Normal University, Huainan, Anhui Province 232038, China.
  • Wang CR; Department of Bioengineering, Huainan Normal University, Huainan, Anhui Province 232038, China.
  • Wang SC; Department of Bioengineering, Huainan Normal University, Huainan, Anhui Province 232038, China.
  • Miao G; Key Laboratory of Bioresource and Environmental Biotechnology of Anhui Higher Education Institutes, Huainan Normal University, Huainan, Anhui Province 232038, China.
Plant Physiol ; 195(3): 1835-1850, 2024 Jun 28.
Article em En | MEDLINE | ID: mdl-38535832
ABSTRACT
Plant transporters regulating the distribution of secondary metabolites play critical roles in defending against pathogens, insects, and interacting with beneficial microbes. The phosphorylation of these transporters can alter their activity, stability, and intracellular protein trafficking. However, the regulatory mechanism underlying this modification remains elusive. In this study, we discovered two orthologs of mammalian PKA, PKG, and PKC (AGC) kinases, oxidative signal-inducible 1 (OXI1) and its closest homologue, AGC subclass 2 member 2 (AGC2-2; 75% amino acid sequence identity with OXI1), associated with the extracellular secretion of camalexin and Arabidopsis (Arabidopsis thaliana) resistance to Pseudomonas syringae, and Botrytis cinerea. These kinases can undergo in vitro kinase reactions with three pleiotropic drug resistance (PDR) transporters PDR6, PDR8, and PDR12. Moreover, our investigation confirmed PDR6 interaction with OXI1 and AGC2-2. By performing LC-MS/MS and parallel reaction monitoring, we identified the phosphorylation sites on PDR6 targeted by these kinases. Notably, chitin-induced PDR6 phosphorylation at specific residues, namely S31, S33, S827, and T832. Additional insights emerged by expressing dephosphorylated PDR6 variants in a pdr6 mutant background, revealing that the target residues S31, S33, and S827 promote PDR6 efflux activity, while T832 potentially contributes to PDR6 stability within the plasma membrane. The findings of this study elucidate partial mechanisms involved in the activity regulation of PDR-type transporters, providing valuable insights for their potential application in future plant breeding endeavors.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doenças das Plantas / Tiazóis / Arabidopsis / Botrytis / Proteínas de Arabidopsis / Pseudomonas syringae / Resistência à Doença Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doenças das Plantas / Tiazóis / Arabidopsis / Botrytis / Proteínas de Arabidopsis / Pseudomonas syringae / Resistência à Doença Idioma: En Ano de publicação: 2024 Tipo de documento: Article