scholarly journals Constitutive Activation of Leucine-Rich Repeat Receptor Kinase Signaling Pathways by BAK1-INTERACTING RECEPTOR-LIKE KINASE3 Chimera

2020 ◽  
Vol 32 (10) ◽  
pp. 3311-3323
Author(s):  
Ulrich Hohmann ◽  
Priya Ramakrishna ◽  
Kai Wang ◽  
Laura Lorenzo-Orts ◽  
Joel Nicolet ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Receptor Kinase ◽  
Leucine Rich Repeat ◽  
Kinase Signaling ◽  
Constitutive Activation ◽  
Receptor Kinase Signaling

Receptor Kinase Signaling Pathways in Plant-Microbe Interactions

2012 ◽  
Vol 50 (1) ◽  
pp. 451-473 ◽  
Author(s):  
Meritxell Antolín-Llovera ◽  
Martina K. Ried ◽  
Andreas Binder ◽  
Martin Parniske
Keyword(s):  
Signaling Pathways ◽  
Receptor Kinase ◽  
Kinase Signaling ◽  
Microbe Interactions ◽  
Receptor Kinase Signaling

scholarly journals Emerging mechanisms to fine-tune receptor kinase signaling specificity

2020 ◽  
Vol 57 ◽  
pp. 41-51 ◽  
Author(s):  
Sergio Galindo-Trigo ◽  
Patrick Blümke ◽  
Rüdiger Simon ◽  
Melinka A Butenko
Keyword(s):  
Receptor Kinase ◽  
Kinase Signaling ◽  
Signaling Specificity ◽  
Receptor Kinase Signaling ◽  
Fine Tune

scholarly journals Organization of the Receptor-Kinase Signaling Array That RegulatesEscherichia coliChemotaxis

2002 ◽  
Vol 277 (39) ◽  
pp. 36748-36754 ◽  
Author(s):  
Mikhail N. Levit ◽  
Thorsten W. Grebe ◽  
Jeffry B. Stock
Keyword(s):  
Receptor Kinase ◽  
Kinase Signaling ◽  
Receptor Kinase Signaling

scholarly journals Constitutive activation of leucine-rich repeat receptor kinase signaling pathways by BAK1-interacting receptor-like kinase 3 chimera

2020 ◽  
Author(s):  
Ulrich Hohmann ◽  
Priya Ramakrishna ◽  
Kai Wang ◽  
Laura Lorenzo-Orts ◽  
Joel Nicolet ◽  
...  
Keyword(s):  
Receptor Activation ◽  
Activation Mechanism ◽  
Signaling Proteins ◽  
Receptor Kinase ◽  
Leucine Rich Repeat ◽  
Protein Ligands ◽  
Receptor Like Kinase ◽  
Transgenic Lines ◽  
Receptor Kinase Signaling ◽  
Membrane Signaling

AbstractReceptor kinases with extracellular leucine-rich repeat domains (LRR-RKs) form the largest group of membrane signaling proteins in plants. LRR-RKs can sense small molecule, peptide or protein ligands, and may be activated by ligand-induced interaction with a shape complementary SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) co-receptor kinase. We have previously shown that SERKs can also form constitutive, ligand-independent complexes with the LRR ectodomains of BAK1-interacting receptor-like kinase 3 (BIR3) receptor pseudokinases, negative regulators of LRR-RK signaling. Here we report that receptor chimaera in which the extracellular LRR domain of BIR3 is fused to the cytoplasmic kinase domains of the SERK-dependent LRR-RKs BRASSINOSTEROID INSENSITIVE1, HAESA and ERECTA form tight complexes with endogenous SERK co-receptors in the absence of ligand stimulus. Expression of these chimaera under the control of the endogenous promoter of the respective LRR-RK leads to strong gain-of-function brassinosteroid, floral abscission and stomatal patterning phenotypes, respectively. Importantly, a BIR3-GSO1/SGN3 chimera can partially complement sgn3 Casparian strip formation phenotypes, suggesting that GSO1/SGN3 receptor activation is also mediated by SERK proteins. Collectively, our protein engineering approach may be used to elucidate the physiological functions of orphan LRR-RKs and to identify their receptor activation mechanism in single transgenic lines.

Abstract 1982: TGF-beta induced SIK cooperates with Smurf2 to negatively regulate type I receptor kinase signaling

2011 ◽  
Author(s):  
Michael Vanlandewijck ◽  
Peter Lönn ◽  
Marcin Kowanetz ◽  
Katarzyna Kowanetz ◽  
Christer Bush ◽  
...  
Keyword(s):  
Type I ◽  
Receptor Kinase ◽  
Kinase Signaling ◽  
Tgf Beta ◽  
Receptor Kinase Signaling
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