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A phosphorelay circuit drives extracellular alkalinization in receptor kinase-mediatedimmune and cell wall damage signaling

ABSTRACT: Extracellular alkalinization has long been recognized as a hallmark of plant cell-surfacereceptor activation, including during pattern-triggered immunity (PTI); yet themechanisms driving elicitor-induced alkalinization and its role in plant signaling remainunclear. Here, we demonstrate that inhibition of autoinhibited H+-ATPases (AHAs) isrequired for elicitor-induced extracellular alkalinization. This alkalinization is essentialfor immune and cell wall damage signaling mediated by diverse plasma membrane-localised receptor kinases (RKs) likely through modulation of ligand-receptorinteractions. Mechanistically, RKs transduce elicitor-triggered signaling via thereceptor-like cytoplasmic kinase BOTRYTIS-INDUCED KINASE 1 (BIK1), whichinhibits AHA activity by disrupting AHA-GENERAL REGULATORY FACTOR (GRF)interactions through a conserved phosphorylation event. This phosphorylation-drivenextracellular alkalinization module is required for disease resistance and cell walldamage responses initiated by ligand-RK pairs. Our findings uncover a conservedphosphorelay circuit that broadly regulates extracellular alkalinization to coordinate RK signaling, illuminating a general mechanism for RK activation and stress resilience.

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ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell

SUBMITTER: FRank Menke

LAB HEAD: Frank Menke

PROVIDER: PXD063345 | Pride | 2026-04-14

REPOSITORIES: Pride

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Project description:modENCODE_submission_2937 This submission comes from a modENCODE project of Michael Snyder. For full list of modENCODE projects, see http://www.genome.gov/26524648 Project Goal: We are identifying the DNA binding sites for 300 transcription factors in C. elegans. Each transcription factor gene is tagged with the same GFP fusion protein, permitting validation of the gene's correct spatio-temporal expression pattern in transgenic animals. Chromatin immunoprecipitation on each strain is peformed using an anti-GFP antibody, and any bound DNA is deep-sequenced using Solexa GA2 technology. For data usage terms and conditions, please refer to http://www.genome.gov/27528022 and http://www.genome.gov/Pages/Research/ENCODE/ENCODEDataReleasePolicyFinal2008.pdf EXPERIMENT TYPE: CHIP-seq. BIOLOGICAL SOURCE: Strain: OP124(official name : OP124 genotype : unc-119(ed3); wgIs124(aha-1::TY1 EGFP FLAG;unc-119) outcross : 3 mutagen : Bombard tags : GFP::3xFlag description : This strain's transgene was constructed by Mihail Sarov at the Max Planck Institute for Cell Biology in Tubiginen using Tony Hyman's recombineering pipeline. The resulting plasmid was used for biolistic transformation of an unc-119(ed3) strain. The AHA-1::EGFP fusion protein is expressed in the correct aha-1 spatio-temporal expression pattern. This strain was used for ChIP-seq experiments to map the in vivo binding sites for the AHA-1 transcription factor. made_by : R. Waterston and S. Kim ); Developmental Stage: fed L1; Genotype: unc-119(ed3); wgIs124(aha-1::TY1 EGFP FLAG;unc-119); Sex: Hermaphrodite; EXPERIMENTAL FACTORS: Developmental Stage fed L1; Target gene aha-1; Strain OP124(official name : OP124 genotype : unc-119(ed3); wgIs124(aha-1::TY1 EGFP FLAG;unc-119) outcross : 3 mutagen : Bombard tags : GFP::3xFlag description : This strain's transgene was constructed by Mihail Sarov at the Max Planck Institute for Cell Biology in Tubiginen using Tony Hyman's recombineering pipeline. The resulting plasmid was used for biolistic transformation of an unc-119(ed3) strain. The AHA-1::EGFP fusion protein is expressed in the correct aha-1 spatio-temporal expression pattern. This strain was used for ChIP-seq experiments to map the in vivo binding sites for the AHA-1 transcription factor. made_by : R. Waterston and S. Kim ); temp (temperature) 20 degree celsius

Project description:modENCODE_submission_3069 This submission comes from a modENCODE project of Michael Snyder. For full list of modENCODE projects, see http://www.genome.gov/26524648 Project Goal: We are identifying the DNA binding sites for 300 transcription factors in C. elegans. Each transcription factor gene is tagged with the same GFP fusion protein, permitting validation of the gene's correct spatio-temporal expression pattern in transgenic animals. Chromatin immunoprecipitation on each strain is peformed using an anti-GFP antibody, and any bound DNA is deep-sequenced using Solexa GA2 technology. For data usage terms and conditions, please refer to http://www.genome.gov/27528022 and http://www.genome.gov/Pages/Research/ENCODE/ENCODEDataReleasePolicyFinal2008.pdf EXPERIMENT TYPE: CHIP-seq. BIOLOGICAL SOURCE: Strain: OP124(official name : OP124 genotype : unc-119(ed3); wgIs124(aha-1::TY1 EGFP FLAG;unc-119) outcross : 3 mutagen : Bombard tags : GFP::3xFlag description : This strain's transgene was constructed by Mihail Sarov at the Max Planck Institute for Cell Biology in Tubiginen using Tony Hyman's recombineering pipeline. The resulting plasmid was used for biolistic transformation of an unc-119(ed3) strain. The AHA-1::EGFP fusion protein is expressed in the correct aha-1 spatio-temporal expression pattern. This strain was used for ChIP-seq experiments to map the in vivo binding sites for the AHA-1 transcription factor. made_by : R. Waterston and S. Kim ); Developmental Stage: L4; Genotype: unc-119(ed3); wgIs124(aha-1::TY1 EGFP FLAG;unc-119); Sex: Hermaphrodite; EXPERIMENTAL FACTORS: Developmental Stage L4; Target gene aha-1; Strain OP124(official name : OP124 genotype : unc-119(ed3); wgIs124(aha-1::TY1 EGFP FLAG;unc-119) outcross : 3 mutagen : Bombard tags : GFP::3xFlag description : This strain's transgene was constructed by Mihail Sarov at the Max Planck Institute for Cell Biology in Tubiginen using Tony Hyman's recombineering pipeline. The resulting plasmid was used for biolistic transformation of an unc-119(ed3) strain. The AHA-1::EGFP fusion protein is expressed in the correct aha-1 spatio-temporal expression pattern. This strain was used for ChIP-seq experiments to map the in vivo binding sites for the AHA-1 transcription factor. made_by : R. Waterston and S. Kim ); temp (temperature) 20 degree celsius

			Action	DRS
	Biosample_names_table_PRIDE.xlsx	Xlsx
	F173320.dat	Other
	F173321.dat	Other
	F173322.dat	Other
	F173323.dat	Other

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A phosphorelay circuit drives extracellular alkalinization in receptor kinase-mediatedimmune and cell wall damage signaling

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