1. G-protein coupling and nuclear translocation of the human abscisic acid receptor LANCL2
- Author
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Cesare Usai, Chiara Fresia, Valeria Booz, Laura Sturla, Antonio De Flora, Elena Zocchi, Mattia Pesce, Tiziana Vigliarolo, Lucrezia Guida, Melody Di Bona, and Santina Bruzzone
- Subjects
0301 basic medicine ,G protein ,Lipoylation ,Gi alpha subunit ,Active Transport, Cell Nucleus ,Biology ,Article ,MECHANISMS ,ACTIVATION ,03 medical and health sciences ,chemistry.chemical_compound ,Glucose homeostasis ,Humans ,Receptor ,Abscisic acid ,Nuclear receptor co-repressor 1 ,Myristoylation ,Cell Nucleus ,MEDICINAL APPLICATIONS ,Multidisciplinary ,IDENTIFICATION ,Peripheral membrane protein ,Cell Membrane ,Membrane Proteins ,Nuclear Proteins ,food and beverages ,LOCALIZATION ,MYRISTOYLATION ,Phosphate-Binding Proteins ,3. Good health ,030104 developmental biology ,HEK293 Cells ,Biochemistry ,chemistry ,CELLS ,2ND-MESSENGER ,BIOCHEMISTRY ,Abscisic Acid ,HeLa Cells ,CYCLIC ADP-RIBOSE - 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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