Calcium/calmodulin inhibition of the Arabidopsis BRASSINOSTEROID-INSENSITIVE 1 receptor kinase provides a possible link between calcium and brassinosteroid signalling.

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  • Additional Information
    • Source:
      Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R Publication Model: Print Cited Medium: Internet ISSN: 1470-8728 (Electronic) Linking ISSN: 02646021 NLM ISO Abbreviation: Biochem J Subsets: MEDLINE
    • Publication Information:
      Original Publication: London, UK : Published by Portland Press on behalf of the Biochemical Society
    • Subject Terms:
      Calcium Signaling*/drug effects; Arabidopsis/*metabolism ; Arabidopsis Proteins/*metabolism ; Brassinosteroids/*metabolism ; Calcium/*metabolism ; Calmodulin/*metabolism ; Protein Kinases/*metabolism; Arabidopsis/drug effects ; Arabidopsis/genetics ; Arabidopsis Proteins/genetics ; Calcium/antagonists & inhibitors ; Calmodulin/antagonists & inhibitors ; Calmodulin/genetics ; Phosphorylation ; Protein Binding ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Kinases/genetics
    • Abstract:
      The receptor kinase BRI1 (BRASSINOSTEROID-INSENSITIVE 1) is a key component in BR (brassinosteroid) perception and signal transduction, and has a broad impact on plant growth and development. In the present study, we demonstrate that Arabidopsis CaM (calmodulin) binds to the recombinant cytoplasmic domain of BRI1 in a Ca2+-dependent manner in vitro. In silico analysis predicted binding to Helix E of the BRI1 kinase subdomain VIa and a synthetic peptide based on this sequence interacted with Ca2+/CaM. Co-expression of CaM with the cytoplasmic domain of BRI1 in Escherichia coli strongly reduced autophosphorylation of BRI1, in particular on tyrosine residues, and also reduced the BRI1-mediated transphosphorylation of E. coli proteins on tyrosine, threonine and presumably serine residues. Several isoforms of CaM and CMLs (CaM-like proteins) were more effective (AtCaM6, AtCaM7 and AtCML8, where At is Arabidopsis thaliana) than others (AtCaM2, AtCaM4 and AtCML11) when co-expressed with BRI1 in E. coli. These results establish a novel assay for recombinant BRI1 transphosphorylation activity and collectively uncover a possible new link between Ca2+ and BR signalling.
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    • Accession Number:
      0 (Arabidopsis Proteins)
      0 (Brassinosteroids)
      0 (Calmodulin)
      0 (Protein Isoforms)
      EC 2.7.- (Protein Kinases)
      EC 2.7.11.1 (BRI1 protein, Arabidopsis)
      SY7Q814VUP (Calcium)
    • Publication Date:
      Date Created: 20120208 Date Completed: 20120514 Latest Revision: 20211021
    • Publication Date:
      20221213
    • Accession Number:
      PMC3316158
    • Accession Number:
      10.1042/BJ20111871
    • Accession Number:
      22309147