Proteomics

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Perception of a conserved family of plant signaling peptides by the receptor kinase HSL3


ABSTRACT: Plant genomes encode hundreds of secreted peptides; however, relatively few have been characterised. We report here an uncharacterised, stress-induced family of plant signalling peptides, which we call CTNIPs. Based on the role of the common co-receptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) in CTNIP-induced responses, we identified the orphan receptor kinase HAESA-LIKE 3 (HSL3) as the CTNIP receptor via a proteomics approach. CTNIP binding, ligand-triggered complex formation with BAK1, and induced downstream responses all involve HSL3. Notably, the HSL3-CTNIP signalling module is evolutionary ancient, predating the divergence of extant angiosperms. Definition of this signalling module will help establish its physiological role and provides a resource to understand further receptor-ligand co-evolution.

INSTRUMENT(S): Orbitrap Fusion

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

TISSUE(S): Plant Cell, Leaf

SUBMITTER: FRank Menke  

LAB HEAD: Frank L.H. Menke

PROVIDER: PXD029264 | Pride | 2022-06-10

REPOSITORIES: Pride

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BBR191010_r01.raw Raw
BBR191010_r01__F147019_.mzid.gz Mzid
BBR191010_r01__F147019_.mzid_BBR191010_r01__F147019_.MGF Mzid
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Publications

Perception of a conserved family of plant signalling peptides by the receptor kinase HSL3.

Rhodes Jack J   Roman Andra-Octavia AO   Bjornson Marta M   Brandt Benjamin B   Derbyshire Paul P   Wyler Michele M   Schmid Marc W MW   Menke Frank L H FLH   Santiago Julia J   Zipfel Cyril C  

eLife 20220526


Plant genomes encode hundreds of secreted peptides; however, relatively few have been characterised. We report here an uncharacterised, stress-induced family of plant signalling peptides, which we call CTNIPs. Based on the role of the common co-receptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) in CTNIP-induced responses, we identified in <i>Arabidopsis thaliana</i> the orphan receptor kinase HAESA-LIKE 3 (HSL3) as the CTNIP receptor via a proteomics approach. CTNIP-binding, ligan  ...[more]

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