Abstract
Detailed phenotypic characterization reveals that several BAK1 fusion proteins with C-terminal tags strongly impair complementation of bak1 null mutants with respect to responsiveness to the bacterial pathogen-associated molecular patterns flagellin and EF-Tu. This raises concerns about the widespread use of such protein variants of this important regulatory Leu-rich repeat receptor-like kinase (RLK) for functional analyses of RLK-based signaling.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Arabidopsis / drug effects
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Arabidopsis / genetics
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Arabidopsis / metabolism
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Arabidopsis Proteins / genetics*
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Arabidopsis Proteins / metabolism*
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Brassinosteroids / metabolism*
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Flagellin / metabolism
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Flagellin / pharmacology
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Mutation
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Peptide Elongation Factor Tu / metabolism
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Peptide Elongation Factor Tu / pharmacology
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Plants, Genetically Modified
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Protein Kinases / metabolism
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Protein Serine-Threonine Kinases / genetics*
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Protein Serine-Threonine Kinases / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism*
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Signal Transduction
Substances
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Arabidopsis Proteins
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Brassinosteroids
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Recombinant Fusion Proteins
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Flagellin
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Protein Kinases
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BAK1 protein, Arabidopsis
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FLS2 protein, Arabidopsis
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BRI1 protein, Arabidopsis
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Protein Serine-Threonine Kinases
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Peptide Elongation Factor Tu