Related Experiment Video
Updated: Jun 15, 2025
07:34
Author Spotlight: Soybean Hairy Root Transformation for the Analysis of Gene Function
Published on: May 5, 2023
3.5K
SymRK Regulates G-Protein Signaling During Nodulation in Soybean (Glycine max) by Modifying RGS Phosphorylation and
Swarup Roy Choudhury1,2, Sona Pandey1
1Donald Danforth Plant Science Center, St. Louis, MO 63132, U.S.A.
Molecular Plant-Microbe Interactions : MPMI
|August 21, 2024
Summary
Soybean nodule formation involves G-protein signaling. Receptor kinases like NFR1 and SymRK phosphorylate RGS proteins, enhancing their activity to regulate G-protein signaling and promote symbiotic nodulation.
Area of Science:
- Plant molecular biology
- Plant-microbe interactions
- Nitrogen fixation
Background:
- Leguminous plants and rhizobia form symbiotic root nodules through molecular dialogue.
- Nodulation is initiated by root hair epidermal cell receptors.
- Heterotrimeric G-proteins and regulators of G-protein signaling (RGS) link receptors to downstream pathways in soybean nodulation.
Purpose of the Study:
- To investigate the role of Symbiosis receptor-like kinases (SymRK) in regulating G-protein signaling during soybean nodulation.
- To elucidate the interaction between SymRK, Nod factor receptor 1 (NFR1), and RGS proteins.
- To determine the physiological relevance of RGS protein phosphorylation in nodule formation.
Main Methods:
- Investigated protein-protein interactions between SymRK, NFR1, and RGS proteins.
- Assessed the effect of SymRK and NFR1 on RGS protein phosphorylation.
- Measured the activity of phosphorylated RGS proteins in GTP hydrolysis.
- Overexpressed a phospho-mimic RGS protein in soybean to evaluate its effect on nodule formation.
Main Results:
- SymRK, similar to NFR1, interacts with and phosphorylates RGS proteins.
- Phosphorylation enhances RGS protein activity, promoting GTP hydrolysis by Gα.
- This leads to the inactivation of the Gα subunit, favoring nodule development.
- Overexpression of a phospho-mimic RGS protein significantly enhances soybean nodule formation.
Conclusions:
- SymRK and NFR1 coordinate to phosphorylate RGS proteins, fine-tuning G-protein signaling.
- This regulatory mechanism ensures adequate nodulation by inactivating negative regulators.
- The findings reveal a complex interplay of receptors and RGS proteins in controlling symbiotic nodule development.
Keywords:
RGS proteinsRLKSymRKheterotrimeric G-proteinsnodulationprotein-protein interactionreceptor-mediated phosphorylationregulator of G-protein signalingsoybean (Glycine max)symbiosis-related receptor-like kinaseMore Related Videos
Related Concept Videos
01:25Cell Signaling in Plants
5.6K
Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
5.6K
01:22Activation and Inactivation of G Proteins
6.9K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
6.9K
01:24Small GTPases - Ras and Rho
3.9K
Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Three regulatory proteins control their activity:
3.9K
01:09GPCRs Regulate Adenylyl Cylase Activity
5.4K
Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
5.4K
01:16TGF - β Signaling Pathway
7.3K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
7.3K
01:22Amplifying Signals via Enzymatic Cascade
8.4K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
8.4K