NDLI: pH Regulation by NHX-Type Antiporters Is Required for Receptor-Mediated Protein Trafficking to the Vacuole in Arabidopsis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Reguera, Maria Bassil, Elias Tajima, Hiromi Wimmer, Monika Chanoca, Alexandra Otegui, Marisa S. Paris, Nadine Blumwald, Eduardo
Description	Author Affiliation: Reguera M ( Department of Plant Sciences, University of California, Davis, California 95616.); Bassil E ( Department of Plant Sciences, University of California, Davis, California 95616.); Tajima H ( Department of Plant Sciences, University of California, Davis, California 95616.); Wimmer M ( Institute of Crop Science and Resource Conservation, Division of Plant Nutrition, University of Bonn, D-53115 Bonn, Germany.); Chanoca A ( Departments of Botany and Genetics, University of Wisconsin, Madison, Wisconsin 53706.); Otegui MS ( Departments of Botany and Genetics, University of Wisconsin, Madison, Wisconsin 53706.); Paris N ( Biochemistry and Plant Molecular Biology Laboratory, Unité Mixte de Recherche 5004, 34060 Montpellier, France.); Blumwald E ( Department of Plant Sciences, University of California, Davis, California 95616 eblumwald@ucdavis.edu.)
Abstract	Protein trafficking requires proper ion and pH homeostasis of the endomembrane system. The NHX-type Na(+)/H(+) antiporters NHX5 and NHX6 localize to the Golgi, trans-Golgi network, and prevacuolar compartments and are required for growth and trafficking to the vacuole. In the nhx5 nhx6 T-DNA insertional knockouts, the precursors of the 2S albumin and 12S globulin storage proteins accumulated and were missorted to the apoplast. Immunoelectron microscopy revealed the presence of vesicle clusters containing storage protein precursors and vacuolar sorting receptors (VSRs). Isolation and identification of complexes of VSRs with unprocessed 12S globulin by 2D blue-native PAGE/SDS-PAGE indicated that the nhx5 nhx6 knockouts showed compromised receptor-cargo association. In vivo interaction studies using bimolecular fluorescence complementation between VSR2;1, aleurain, and 12S globulin suggested that nhx5 nhx6 knockouts showed a significant reduction of VSR binding to both cargoes. In vivo pH measurements indicated that the lumens of VSR compartments containing aleurain, as well as the trans-Golgi network and prevacuolar compartments, were significantly more acidic in nhx5 nhx6 knockouts. This work demonstrates the importance of NHX5 and NHX6 in maintaining endomembrane luminal pH and supports the notion that proper vacuolar trafficking and proteolytic processing of storage proteins require endomembrane pH homeostasis.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
DOI	10.1105/tpc.114.135699
Journal	THE PLANT CELL ONLINE
Issue Number	4
Volume Number	27
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2015-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Arabidopsis Proteins Metabolism Arabidopsis Vacuoles Genetics Electrophoresis, Polyacrylamide Gel Gene Expression Regulation, Plant Protein Transport Physiology Trans-golgi Network Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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pH Regulation by NHX-Type Antiporters Is Required for Receptor-Mediated Protein Trafficking to the Vacuole in Arabidopsis

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