ArticlePlant physiology2015
Membrane-localized extra-large G proteins and Gbg of the heterotrimeric G proteins form functional complexes engaged in plant immunity in Arabidopsis.
Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 120 citations in OpenAlex.
- Arabidopsis Heterotrimeric G Beta Variants Shape Plant Development and Modulate Responses to Endoplasmic Reticulum Stress and Salt Stress.Plant, cell & environment · 2026Article
- Article
- Phosphovariants of the canonical heterotrimeric Gα protein, GPA1, differentially affect G protein activity and Arabidopsis development.bioRxiv : the preprint server for biology · 2026Article
- Extra-large G proteins and their roles in plant development and responses to environmental stresses.Frontiers in plant science · 2026Review
- Flagellin sensing, signaling, and immune responses in plants.Plant communications · 2025Review
- Phosphorylation-activated G protein signaling stabilizes TCP14 and JAZ3 to repress JA signaling and enhance plant immunity.Molecular plant · 2025Article
- Overexpression ofPlants (Basel, Switzerland) · 2024Article
- Conserved Role of Heterotrimeric G Proteins in Plant Defense and Cell Death Progression.Genes · 2024Article
- Review
- An atypical heterotrimeric Gα and its interactome suggest an extra-large role in overcoming abiotic and biotic stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Review
- Extra-large G proteins have extra-large effects on agronomic traits and stress tolerance in maize and rice.Trends in plant science · 2023Review
- The interplay of GTP-binding protein AGB1 with ER stress sensors IRE1a and IRE1b modulates Arabidopsis unfolded protein response and bacterial immunity.Plant signaling & behavior · 2022Article
- EXTRA LARGE G-PROTEIN2 mediates cell death and hyperimmunity in the chitin elicitor receptor kinase 1-4 mutant.Plant physiology · 2022Article
- G-Protein Phosphorylation: Aspects of Binding Specificity and Function in the Plant Kingdom.International journal of molecular sciences · 2022Review
- Heterotrimeric G Protein Signaling in Abiotic Stress.Plants (Basel, Switzerland) · 2022Review
- Review
- Spliceostatin C, a component of a microbial bioherbicide, is a potent phytotoxin that inhibits the spliceosome.Frontiers in plant science · 2022Article
- Tomato and cotton G protein beta subunit mutants display constitutive autoimmune responses.Plant direct · 2021Article
- Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021Review
- Extra-large G-proteins influence plant response to Sclerotinia sclerotiorum by regulating glucosinolate metabolism in Brassica juncea.Molecular plant pathology · 2021Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In animals, heterotrimeric G proteins, comprising Ga, Gb, and Gg subunits, are molecular switches whose function tightly depends on Ga and Gbg interaction. Intriguingly, in Arabidopsis (Arabidopsis thaliana), multiple defense responses involve Gbg, but not Ga. We report here that the Gbg dimer directly partners with extra-large G proteins (XLGs) to mediate plant immunity. Arabidopsis mutants deficient in XLGs, Gb, and Gg are similarly compromised in several pathogen defense responses, including disease development and production of reactive oxygen species. Genetic analysis of double, triple, and quadruple mutants confirmed that XLGs and Gbg functionally interact in the same defense signaling pathways. In addition, mutations in XLG2 suppressed the seedling lethal and cell death phenotypes of BRASSINOSTEROID INSENSITIVE1-associated receptor kinase1-interacting receptor-like kinase1 mutants in an identical way as reported for Arabidopsis Gb-deficient mutants. Yeast (Saccharomyces cerevisiae) three-hybrid and bimolecular fluorescent complementation assays revealed that XLG2 physically interacts with all three possible Gbg dimers at the plasma membrane. Phylogenetic analysis indicated a close relationship between XLGs and plant Ga subunits, placing the divergence point at the dawn of land plant evolution. Based on these findings, we conclude that XLGs form functional complexes with Gbg dimers, although the mechanism of action of these complexes, including activation/deactivation, must be radically different form the one used by the canonical Ga subunit and are not likely to share the same receptors. Accordingly, XLGs expand the repertoire of heterotrimeric G proteins in plants and reveal a higher level of diversity in heterotrimeric G protein signaling.
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