1. G-protein coupling and nuclear translocation of the human abscisic acid receptor LANCL2.
- Author
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Fresia C, Vigliarolo T, Guida L, Booz V, Bruzzone S, Sturla L, Di Bona M, Pesce M, Usai C, De Flora A, and Zocchi E
- Subjects
- Active Transport, Cell Nucleus drug effects, Active Transport, Cell Nucleus genetics, Cell Membrane genetics, Cell Nucleus genetics, HEK293 Cells, HeLa Cells, Humans, Lipoylation drug effects, Membrane Proteins genetics, Nuclear Proteins genetics, Phosphate-Binding Proteins, Abscisic Acid pharmacology, Cell Membrane metabolism, Cell Nucleus metabolism, Lipoylation physiology, Membrane Proteins metabolism, Nuclear Proteins metabolism
- Abstract
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 Gi 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.
- Published
- 2016
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