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PAMP Signals in Plant Innate Immunity pp 163–205Cite as

G-Proteins as Molecular Switches in Signal Transduction

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Part of the book series: Signaling and Communication in Plants ((SIGCOMM,volume 21))

Abstract

Guanosine triphosphate (GTP)-binding proteins (G-proteins) are the regulatory GTPases that have the ability to bind GTP and hydrolyze it to guanosine diphosphate (GDP). GDP locks G proteins into their inactive state, while GTP locks G-proteins into their activated state. Active or inactive states of G-proteins depend on the binding of GTP or GDP, respectively. G-proteins have been found to be key players in plant innate immunity. The GTPases act as molecular switches controlling the transmission of extracellular signals like pathogen-associated molecular patterns (PAMPs) to intracellular signaling pathways. The PAMPs have been shown to activate GTP binding to G-protein. The GTPase is normally inactive. The PAMP stimulates exchange of GTP for GDP and thus converts the G-proteins from their inactive state to their active state. Upon stimulation by an upstream PAMP signal, a guanine nucleotide exchange factor (GEF) converts the GDP-bound inactive form into the GTP-bound active form through GDP/GTP replacement. Through its effector domain, the GTP form interacts with specific downstream effector proteins. The GTP form exhibits a weak intrinsic GTPase activity for GTP hydrolysis, requiring a GTPase-activating protein (GAP) for efficient deactivation. Most small GTPases cycle between membrane-bound and cytosolic forms. Only membrane-associated GTPases can be activated by GEF and their removal by a cytosolic factor called guanine nucleotide dissociation inhibitor (GDI) negatively regulates these GTPases.

G-proteins include two major subfamilies: heterotrimeric G-proteins and small G-proteins (also called small GTPases). The heterotrimeric G-proteins contain Gα-, Gβ-, and Gγ- subunits. The small G-proteins are monomeric G-proteins and they appear to be similar to α-subunits, operating without the β-, and γ-subunits. Both classes of G-proteins use the GTP/GDP cycle as a molecular switch for signal transduction. Both heteromeric and monomeric small G-proteins trigger immune responses by activating several immune signaling systems. These include Ca2+ channel activation, K+ channel regulation, generation of reactive oxygen species through activation of NADPH oxidase, regulation of redox signaling, activation of nitric oxide (NO) signaling system, activation of mitogen-activated protein kinase (MAPK) signaling cascade, activation of phospholipases, efflux of vacuolar H+, biosynthesis of polyamines, biosynthesis of phosphatidic acid and programmed cell death. G-proteins also activate various plant hormone signaling systems including salicylic acid-, jasmonic acid-, ethylene-, abscisic acid-, auxin-, brassinosteroid-, and gibberellic acid- mediated signaling systems. The different subunits in heterotrimeric G-proteins and the monomeric small G-proteins may behave differently in activating defense responses against various pathogens. Ability of G-proteins to trigger immune responses also varies depending upon the type of invading pathogen.

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  1. Plant Pathology, Tamil Nadu Agricultural University, Coimbatore, Tamil Nadu, India

    P. Vidhyasekaran

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Vidhyasekaran, P. (2014). G-Proteins as Molecular Switches in Signal Transduction. In: PAMP Signals in Plant Innate Immunity. Signaling and Communication in Plants, vol 21. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-7426-1_3

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