G-protein coupling and nuclear translocation of the human abscisic acid receptor LANCL2

• Published in: Scientific reports Vol. 6; no. 1; p. 26658
• Main Authors: Fresia, Chiara, Vigliarolo, Tiziana, Guida, Lucrezia, Booz, Valeria, Bruzzone, Santina, Sturla, Laura, Di Bona, Melody, Pesce, Mattia, Usai, Cesare, De Flora, Antonio, Zocchi, Elena
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 25.05.2016; Nature Publishing Group
• Subjects: 14/19; 14/33; 14/35; 631/337; 631/45; 631/57; 82/1; 82/29; 96/109; 96/21; Abscisic acid; Adenylate cyclase; Glycine; Homeostasis; Humanities and Social Sciences; Immune response; Innate immunity; Localization; Membrane proteins; Membrane vesicles; Mesenchyme; multidisciplinary; Myristoylation; Nuclear transport; Protein transport; Proteins; Science; Signal transduction; Stem cells; Translocation
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep26658

Abscisic acid (ABA), a long known phytohormone, has been recently demonstrated to be present also in humans, where it targets cells of the innate immune response, mesenchymal and hemopoietic stem cells and cells involved in the regulation of systemic glucose homeostasis. LANCL2, a peripheral membrane protein, is the mammalian ABA receptor. We show that N-terminal glycine myristoylation causes LANCL2 localization to the plasmamembrane and to cytoplasmic membrane vesicles, where it interacts with the α subunit of a G i protein and starts the ABA signaling pathway via activation of adenylate cyclase. Demyristoylation of LANCL2 by chemical or genetic means triggers its nuclear translocation. Nuclear enrichment of native LANCL2 is also induced by ABA treatment. Therefore human LANCL2 is a non-transmembrane G protein-coupled receptor susceptible to hormone-induced nuclear translocation.