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Literature summary extracted from

  • Choudhury, S.R.; Pandey, S.
    Phosphorylation-dependent regulation of G-protein cycle during nodule formation in soybean (2015), Plant Cell, 27, 3260-3276 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.6.5.1 G196S the mutation in Galpha1 makes the enzyme nearly incapable of being deactivated by RGS protein Glycine max
3.6.5.1 additional information Galpha-RNAi mutant roots exhibit significantly higher whereas RGS-RNAi hairy roots exhibit significantly lower root hair deformation, respectively, compared with the EV control hairy roots. No additional effect on overall root length or lateral root formation is seen in Galpha-RNAi or RGS-RNAi roots Glycine max
3.6.5.1 Q223L the mutation in a conserved glutamine residue that is important for the GTPase activity of Galpha proteins (in Galpha1) results in a GTPase activity-lacking, constitutively active protein Glycine max

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.5.1 Mg2+ required Glycine max

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.5.1 GTP + H2O Glycine max
-
 GDP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.1 Glycine max
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.6.5.1 phosphoprotein role of Nod factor receptor 1 (NFR1)-mediated phosphorylation in regulation of the G-protein cycle during nodulation in soybean Glycine max

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.5.1 hairy root
-
 Glycine max
-
3.6.5.1 root
-
 Glycine max
-
3.6.5.1 root nodule
-
 Glycine max
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.1 GTP + H2O
-
 Glycine max GDP + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.5.1 Galpha protein
-
 Glycine max

General Information

EC Number General Information Comment Organism
3.6.5.1 evolution plants also possess relatively fewer G-protein subunits when compared with the mammalian systems. A highly elaborated plant G-protein network is present in soybean where recent genome duplication has led to existence of 4 Galpha, 4 Gbeta, 12 Ggamma, and 2 RGS proteins Glycine max
3.6.5.1 malfunction decreased expression of Gbeta and group I Ggamma genes leads to a significant decrease in nodule number, whereas the converse is true for the overexpression of specific Gbeta and Ggamma genes. Changing the availability of free, active Galpha proteins by modulating the level of the regulatory RGS proteins results in significantly altered nodule numbers. Overexpression of mutant Galpha1Q223L and Galpha1G196S, as confirmed by evaluating the transcript level of the transformed genes, results in a significant decrease in nodule number per transformed root Glycine max
3.6.5.1 metabolism signaling pathways mediated by heterotrimeric G-protein complexes comprising Galpha, Gbeta, and Ggamma subunits and their regulatory RGS (regulator of G-protein signaling) protein are conserved in all eukaryotes. In soybean, phosphorylation-dependent regulation of G-protein cycle during nodule formation exists involving Nod factor receptor 1 (NFR1). The specific Gbeta and Ggamma proteins of a soybean heterotrimeric G-protein complex are involved in regulation of nodulation. 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. Active NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the Galpha 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. The RGS proteins directly interact with, and are phosphorylated by, the NFR1 proteins. Phosphorylation of RGS proteins has important physiological consequences as overexpression of phospho-dead or phospho-mimic versions of RGS proteins results in a significant effect on nodule formation. The RGS protein-mediated acceleration of GTP hydrolysis is proposed to be the key regulatory step of plant G-protein signaling in contrast to mammalian systems where the GDP/GTP exchange mediated by the GPCRs is the rate-limiting step of the G-protein cycle. RGS proteins affect nodulation, they are positive regulators of nodule formation, detailed overview Glycine max
3.6.5.1 physiological function a highly elaborated plant G-protein network is present in soybean where recent genome duplication has led to existence of 4 Galpha, 4 Gbeta, 12 Ggamma, and 2 RGS proteins. G-proteins from soybean have a direct negative role in signaling during nodulation. The Galpha proteins interact with the Nod factor receptors NFR1alpha and NFR1beta. The RGS protein-mediated acceleration of GTP hydrolysis is proposed to be the key regulatory step of plant G-protein signaling in contrast to mammalian systems where the GDP/GTP exchange mediated by the GPCRs is the rate-limiting step of the G-protein cycle Glycine max