Phosphorylation-dependent regulation of G-protein Cycle during nodule formation in Soybean

Swarup Roy Choudhury, Sona Pandey

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

Signaling pathways mediated by heterotrimeric G-protein complexes comprising Ga, Gb, and Gg subunits and their regulatory RGS (Regulator of G-protein Signaling) protein are conserved in all eukaryotes. We have shown that the specific Gb and Gg proteins of a soybean (Glycine max) heterotrimeric G-protein complex are involved in regulation of nodulation. We now demonstrate the role of Nod factor receptor 1 (NFR1)-mediated phosphorylation in regulation of the G-protein cycle during nodulation in soybean. We also show that during nodulation, the G-protein cycle is regulated by the activity of RGS proteins. Lower or higher expression of RGS proteins results in fewer or more nodules, respectively. NFR1 interacts with RGS proteins and phosphorylates them. Analysis of phosphorylated RGS protein identifies specific amino acids that, when phosphorylated, result in significantly higher GTPase accelerating activity. These data point to phosphorylation-based regulation of G-protein signaling during nodule development. We propose that active NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the Ga proteins in their inactive, trimeric conformation, resulting in successful nodule development. Alternatively, RGS proteins might also have a direct role in regulating nodulation because overexpression of their phospho-mimic version leads to partial restoration of nodule formation in nod49 mutants.

Original languageEnglish
Pages (from-to)3260-3276
Number of pages17
JournalPlant Cell
Volume27
Issue number11
DOIs
StatePublished - Nov 2015

Fingerprint

Dive into the research topics of 'Phosphorylation-dependent regulation of G-protein Cycle during nodule formation in Soybean'. Together they form a unique fingerprint.

Cite this