title: G-protein coupling and nuclear translocation of the human abscisic acid receptor LANCL2.
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.
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Chiara
authors.initials: C
authors.lastname: Fresia
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Tiziana
authors.initials: T
authors.lastname: Vigliarolo
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Lucrezia
authors.initials: L
authors.lastname: Guida
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Valeria
authors.initials: V
authors.lastname: Booz
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Santina
authors.initials: S
authors.lastname: Bruzzone
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Laura
authors.initials: L
authors.lastname: Sturla
authors.affiliation: Istituto Italiano di Tecnologia (IIT), Genova, Italy.
authors.forename: Melody
authors.initials: M
authors.lastname: Di Bona
authors.affiliation: Istituto Italiano di Tecnologia (IIT), Genova, Italy.
authors.forename: Mattia
authors.initials: M
authors.lastname: Pesce
authors.affiliation: Institute of Biophysics, National Research Council (CNR), Genova, Italy.
authors.forename: Cesare
authors.initials: C
authors.lastname: Usai
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Antonio
authors.initials: A
authors.lastname: De Flora
authors.affiliation: Department of Experimental Medicine, Section of Biochemistry, University of Genova, Italy.
authors.forename: Elena
authors.initials: E
authors.lastname: Zocchi
mesh_terms: D000040:Abscisic Acid / Q000494:pharmacology*; D021581:Active Transport, Cell Nucleus / Q000187:drug effects / Q000235:genetics; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism*; D002467:Cell Nucleus / Q000235:genetics / Q000378:metabolism*; D057809:HEK293 Cells; D006367:HeLa Cells; D006801:Humans; D054878:Lipoylation / Q000187:drug effects / Q000502:physiology*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D028044:Phosphate-Binding Proteins
chemical_list: C471704:LANCL2 protein, human; D008565:Membrane Proteins; D009687:Nuclear Proteins; D028044:Phosphate-Binding Proteins; D000040:Abscisic Acid