The superfamily of G-protein-coupled receptors (GPCRs) is one of the largest and most diverse family of proteins in mammals. Plants, in contrast to animals, have a greatly simplified repertoire of GPCRs. To date, only AtGCR1 and AtRGS1 have been shown to physically interacts with a plant G-protein. Also, the number of G-protein complex components in plants is dramatically less than in other Eukaryotes. Only one prototypical Ga subunit, one Gbeta and two Ggamma subunits have been identified in A. thaliana and rice. Similarly, there are few known downstream effectors that physicaly interact with either the plant Ga subunit or the Gbetagamma dimer. The best-characterized effector is phospholipase D (PLDalpha1). Besides, the potential Galpha effectors are: cupin-domain protein designated as Atpirin1, prephenate dehydratase--a cytosolic enzyme involved in regulation of the shikimate pathway, and THF1 protein located in plastid membranes. Indirect evidences suggest that Galpha may interact with ion channels and phospholipases A2 and C, whereas Gbetagamma dimer supposedly interacts with a Golgi-localized hexose transporter.
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J Physiol
November 2024
Institute for Molecular Medicine, MSH Medical School Hamburg, Hamburg, Germany.
Volume-regulated anion channels (VRACs) formed by leucin-rich repeat containing 8 (LRRC8) proteins play a pivotal role in regulatory volume decrease by mediating the release of chloride and organic osmolytes. Apart from the regulation of cell volume, LRRC8/VRAC function underlies numerous physiological processes in vertebrate cells including membrane potential regulation, glutamate release and apoptosis. LRRC8/VRACs are also permeable to antibiotics and anti-cancer drugs, representing therefore important therapeutic targets.
View Article and Find Full Text PDFPlant Cell Environ
December 2024
School of Life Sciences, Shaanxi Normal University, Xi'an, Shaanxi, China.
In the investigation of heterotrimeric G protein-mediated signal transduction in planta, their roles in the transmittance of low K stimuli remain to be elucidated. Here, we found that the primary root growth of wild-type Arabidopsis was gradually inhibited with the decrease of external K concentrations, while the primary root of the mutants for G protein β subunit AGB1 and γ subunits AGG1, AGG2 and AGG3 could still grow under low K conditions (LK). Exogenous NAA application attenuated primary root elongation in agb1 and agg1/2/3 but promoted the growth in wild-type seedlings under LK stress.
View Article and Find Full Text PDFBiochim Biophys Acta Biomembr
August 2024
Department of Life Science, Sogang University, 35 Baekbeom-ro, Mapo-gu, Seoul 04107, Republic of Korea. Electronic address:
Ca influx through Ca3.3 T-type channel plays crucial roles in neuronal excitability and is subject to regulation by various signaling molecules. However, our understanding of the partners of Ca3.
View Article and Find Full Text PDFNat Struct Mol Biol
August 2024
Department of Biological Sciences, Purdue University, West Lafayette, IN, USA.
The nine different membrane-anchored adenylyl cyclase isoforms (AC1-9) in mammals are stimulated by the heterotrimeric G protein, Gα, but their response to Gβγ regulation is isoform specific. In the present study, we report cryo-electron microscope structures of ligand-free AC5 in complex with Gβγ and a dimeric form of AC5 that could be involved in its regulation. Gβγ binds to a coiled-coil domain that links the AC transmembrane region to its catalytic core as well as to a region (C) that is known to be a hub for isoform-specific regulation.
View Article and Find Full Text PDFGenes (Basel)
January 2024
School of Agriculture and Food Sciences, University of Queensland, St. Lucia, Brisbane, QLD 4072, Australia.
Programmed cell death (PCD) is a critical process in plant immunity, enabling the targeted elimination of infected cells to prevent the spread of pathogens. The tight regulation of PCD within plant cells is well-documented; however, specific mechanisms remain elusive or controversial. Heterotrimeric G proteins are multifunctional signaling elements consisting of three distinct subunits, Gα, Gβ, and Gγ.
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