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Updated: Sep 6, 2025

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
G-Protein Phosphorylation: Aspects of Binding Specificity and Function in the Plant Kingdom
Celio Cabral Oliveira1,2,3, Alan M Jones3,4, Elizabeth Pacheco Batista Fontes1,2
1Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Viçosa 36570, Brazil.
Abstract:
Plant survival depends on adaptive mechanisms that constantly rely on signal recognition and transduction. The predominant class of signal discriminators is receptor kinases, with a vast member composition in plants. The transduction of signals occurs in part by a simple repertoire of heterotrimeric G proteins, with a core composed of α-, β-, and γ-subunits, together with a 7-transmembrane Regulator G Signaling (RGS) protein. With a small repertoire of G proteins in plants, phosphorylation by receptor kinases is critical in regulating the active state of the G-protein complex. This review describes the in vivo detected phosphosites in plant G proteins and conservation scores, and their in vitro corresponding kinases. Furthermore, recently described outcomes, including novel arrestin-like internalization of RGS and a non-canonical phosphorylation switching mechanism that drives G-protein plasticity, are discussed.
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