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Receptor-Like Kinase Phosphorylation of Arabidopsis Heterotrimeric G-Protein Gα -Subunit AtGPA1.
Jia, Haiyan; Song, Gaoyuan; Werth, Emily G; Walley, Justin W; Hicks, Leslie M; Jones, Alan M.
Afiliação
  • Jia H; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
  • Song G; Department of Plant Pathology and Microbiology, Iowa State University, Ames, IA, 50011, USA.
  • Werth EG; Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
  • Walley JW; Department of Plant Pathology and Microbiology, Iowa State University, Ames, IA, 50011, USA.
  • Hicks LM; Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
  • Jones AM; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
Proteomics ; 19(24): e1900265, 2019 12.
Article em En | MEDLINE | ID: mdl-31693794
As molecular on-off switches, heterotrimeric G protein complexes, comprised of a Gα subunit and an obligate Gßγ dimer, transmit extracellular signals received by G protein-coupled receptors (GPCRs) to cytoplasmic targets that respond to biotic and abiotic stimuli. Signal transduction is modulated by phosphorylation of GPCRs and G protein complexes. In Arabidopsis thaliana, the Gα subunit AtGPA1 is phosphorylated by the receptor-like kinase (RLK) BRI1-associated Kinase 1 (BAK1), but the extent that other RLKs phosphorylates AtGPA1 is unknown. Twenty-two trans-phosphorylation sites on AtGPA1 are mapped by 12 RLKs hypothesized to act in the Arabidopsis G protein signaling pathway. Cis-phosphorylation sites are also identified on these RLKs, some newly shown to be dual specific kinases. Multiple sites are present in the core AtGPA1 functional units, including pSer52 and/or pThr53 of the conserved P-loop that directly binds nucleotide/phosphate, pThr164, and pSer175 from αE helix in the intramolecular domain interface for nucleotide exchange and GTP hydrolysis, and pThr193 and/or pThr194 in Switch I (SwI) that coordinates nucleotide exchange and protein partner binding. Several AtGPA1 S/T phosphorylation sites are potentially nucleotide-dependent phosphorylation patterns, such as Ser52/Thr53 in the P-loop and Thr193 and/or Thr194 in SwI.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Arabidopsis / Regulação da Expressão Gênica de Plantas / Proteínas de Arabidopsis / Subunidades alfa de Proteínas de Ligação ao GTP Idioma: En Revista: Proteomics Assunto da revista: BIOQUIMICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Arabidopsis / Regulação da Expressão Gênica de Plantas / Proteínas de Arabidopsis / Subunidades alfa de Proteínas de Ligação ao GTP Idioma: En Revista: Proteomics Assunto da revista: BIOQUIMICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Estados Unidos