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• W2042829895 abstract "Significance The innate immune response is initiated by the recognition of conserved microbial signatures via membrane-resident receptor complex. The dimerization and phosphorylation of Arabidopsis protein kinase complex FLS2/BAK1/BIK1 is essential to initiate and transduce immune signaling to bacterial flagellin. BIK1, a classic serine/threonine kinase, was found here to be autophosphorylated and transphosphorylated by BAK1 at multiple tyrosine residues to relay plant immune signaling. The essential function of tyrosine kinase activity of BIK1 in plants echoes the function of nonreceptor tyrosine kinases that transduce receptor tyrosine kinase signaling via dimerization and phosphorylation in metazoans. Thus, despite lack of classical tyrosine kinases, tyrosine phosphorylation is also an important regulatory mechanism to control membrane-resident receptor signaling in plants." @default.
• W2042829895 created "2016-06-24" @default.
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• W2042829895 date "2014-02-14" @default.
• W2042829895 modified "2023-10-01" @default.
• W2042829895 title "Tyrosine phosphorylation of protein kinase complex BAK1/BIK1 mediates <i>Arabidopsis</i> innate immunity" @default.
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• W2042829895 doi "https://doi.org/10.1073/pnas.1318817111" @default.
• W2042829895 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3948311" @default.
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