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Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis.
Plant Cell Physiol
November 2024
Structural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, 30 Quai E. Ansermet, Geneva 1211, Switzerland.
Brassinosteroids (BRs) are vital plant steroid hormones sensed at the cell surface by a membrane signaling complex comprising the receptor kinase BRI1 and a SERK family co-receptor kinase. Activation of this complex lead to dissociation of the inhibitor protein BKI1 from the receptor and to differential phosphorylation of BZR1/BES1 transcription factors by the glycogen synthase kinase 3 protein BIN2. Many phosphoproteins of the BR signaling pathway, including BRI1, SERKs, BKI1 and BZR1/BES1 can associate with 14-3-3 proteins.
View Article and Find Full Text PDFBAK-up: the receptor kinase BAK-TO-LIFE 2 enhances immunity when BAK1 is lacking.
Stress Biol
September 2023
ZMBP, University Tübingen, Auf der Morgenstelle 32, Tübingen, 72076, Germany.
BRI1-ASSOCIATED KINASE 1 (BAK1/SERK3) and its closest homolog BAK1-LIKE 1 (BKK1/SERK4) are leucine-rich repeat receptor kinases (LRR-RKs) belonging to the SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) family. They act as co-receptors of various other LRR-RKs and participate in multiple signaling events by complexing and transphosphorylating ligand-binding receptors. Initially identified as the brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1) co-receptor, BAK1 also functions in plant immunity by interacting with pattern recognition receptors.
View Article and Find Full Text PDFHSL1 and BAM1/2 impact epidermal cell development by sensing distinct signaling peptides.
Nat Commun
February 2022
The Plant Signaling Mechanisms Laboratory, Department of Plant Molecular Biology, University of Lausanne, 1015, Lausanne, Switzerland.
The membrane receptor kinases HAESA and HSL2 recognize a family of IDA/IDL signaling peptides to control cell separation processes in different plant organs. The homologous HSL1 has been reported to regulate epidermal cell patterning by interacting with a different class of signaling peptides from the CLE family. Here we demonstrate that HSL1 binds IDA/IDL peptides with high, and CLE peptides with lower affinity, respectively.
View Article and Find Full Text PDFChemical control of receptor kinase signaling by rapamycin-induced dimerization.
Mol Plant
August 2021
Department of Bioenergy Science and Technology, Chonnam National University, Gwangju, Korea; Kumho Life Science Laboratory, Chonnam National University, Gwangju, Korea; Department of Integrative Food, Bioscience and Biotechnology, Chonnam National University, Gwangju, Korea. Electronic address:
Membrane-localized leucine-rich repeat receptor kinases (LRR-RKs) sense diverse extracellular signals, and coordinate and specify cellular functions in plants. However, functional understanding and identification of the cellular signaling of most LRR-RKs remain a major challenge owing to their genetic redundancy, the lack of ligand information, and subtle phenotypes of LRR-RK overexpression. Here, we report an engineered rapamycin-inducible dimerization (RiD) receptor system that triggers a receptor-specific LRR-RK signaling independent of their cognate ligands or endogenous receptors.
View Article and Find Full Text PDFThe SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling.
Nat Plants
June 2018
Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
The leucine-rich repeat receptor kinase (LRR-RK) BRASSINOSTEROID INSENSITIVE 1 (BRI1) requires a shape-complementary SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) co-receptor for brassinosteroid sensing and receptor activation. Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses. The SERK3 elongated (elg) allele maps to the complex interface and shows enhanced brassinosteroid signalling, but surprisingly no tighter binding to the BRI1 ectodomain in vitro.
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