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Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling

ABSTRACT: The structural dynamics of purified wild type and mutant EFR were probed by HDX-MS.

INSTRUMENT(S): Synapt MS

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

SUBMITTER: Yuko Tsutsui

LAB HEAD: Yuko Tsutsui

PROVIDER: PXD049215 | Pride | 2024-06-27

REPOSITORIES: pride

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			Action	DRS
	220822_EFRuncut_exp5_0sec_01_vial01.raw.zip	Raw
	220822_EFRuncut_exp5_0sec_01_vial01_IA_final_peptide.csv	Csv
	220822_EFRuncut_exp5_0sec_02_vial01.raw.zip	Raw
	220822_EFRuncut_exp5_0sec_02_vial01_IA_final_peptide.csv	Csv
	220822_EFRuncut_exp5_0sec_03_vial01.raw.zip	Raw

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Publications

Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling.

Mühlenbeck Henning H Tsutsui Yuko Y Lemmon Mark A MA Bender Kyle W KW Zipfel Cyril C

bioRxiv : the preprint server for biology 20240508

Transmembrane signaling by plant receptor kinases (RKs) has long been thought to involve reciprocal trans-phosphorylation of their intracellular kinase domains. The fact that many of these are pseudokinase domains, however, suggests that additional mechanisms must govern RK signaling activation. Non-catalytic (pseudo)kinase signaling mechanisms have been described in metazoans, but information is scarce for plants. Recently, a non-catalytic function was reported for the leucine-rich repeat (LRR) ...[more]

PMID: 37662281

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