Heterotrimeric G-proteins in plant cell signaling

Heterotrimeric G-proteins, which couple cell surface receptors with internal effectors, are evident in all eukaryotes. Their operation involves receptor activation, GTP/GDP exchange and modulation of effector activity; deactivation occurs by an intrinsic GTPase activity. Structurally, G-proteins comprise three dissimilar subunits; Gα, Gβ and Gγ. The Gα subunit consists of an α-helical and a GTPase domain, the latter is responsible for interaction with Gβγ, receptor and effector. Gβ and Gγ form a tightly associated heterodimer which can also modulate effector activity when released by the activated Gα. Genome sequence and other data suggest that, in plants, there are several (~8-10?) Gα, one or two Gβ and one Gγ. These proteins are expressed throughout the plant, mainly in the plasma membrane and endoplasmic reticulum. In vivo, there is strong evidence for G-protein control of ion channels, particularly K⁺ , in the response pathways to fungal and bacterial pathogens as well as in some aspects of gibberellin, abscisic acid and auxin signaling pathways. Finally, future prospects for understanding plant G-protein linked signaling will rely on new and emerging technologies; these include antisense suppression, gene knockouts, yeast two-hybrid and phage display molecular approaches, intracellular immunization using recombinant single chain antibodies and expression of peptide encoding minigenes.