SymRK regulates G-protein signaling during nodulation in soybean (Glycine max) by modifying RGS phosphorylation and activity.
Mol Plant Microbe Interact
; 2024 Aug 21.
Article
de En
| MEDLINE
| ID: mdl-39167823
ABSTRACT
Molecular inter-species dialogue between leguminous plants and nitrogen-fixing rhizobia results in the development of symbiotic root nodules. This is initiated by several nodulation-related receptors present on the surface of root hair epidermal cells. We have shown previously that specific subunits of heterotrimeric G proteins and their regulatory RGS (regulator of G-protein signaling) proteins act as molecular links between the receptors and downstream components during nodule formation in soybeans. Nod factor receptor 1 (NFR1) interacts with and phosphorylates RGS proteins to regulate the G-protein cycle. Symbiosis receptor-like kinases (SymRK) phosphorylate Gα to make it inactive and unavailable for Gßγ. We now show that like NFR1, SymRK also interacts with the RGS proteins to phosphorylate them. Phosphorylated RGS has higher GTP accelerating activity, which favors conversion of active Gα to its inactive form. Phosphorylation of RGS proteins is physiologically relevant, as overexpression of a phospho-mimic version of RGS protein enhances nodule formation in soybean. These results reveal an intricate fine-tuning of the G-protein signaling during nodulation, where a negative regulator (Gα) is effectively deactivated by RGS due to the concerted efforts of several receptor proteins to ensure adequate nodulation.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Langue:
En
Journal:
Mol Plant Microbe Interact
Sujet du journal:
BIOLOGIA MOLECULAR
/
BOTANICA
/
MICROBIOLOGIA
Année:
2024
Type de document:
Article
Pays de publication:
États-Unis d'Amérique