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Type: Journal article
Title: Rice SPX-Major Facility Superfamily3, a vacuolar phosphate efflux transporter, is involved in maintaining phosphate homeostasis in rice
Author: Wang, C.
Yue, W.
Ying, Y.
Wang, S.
Secco, D.
Liu, Y.
Whelan, J.
Tyerman, S.
Shou, H.
Citation: Plant Physiology, 2015; 169(4):2822-2831
Publisher: American Society of Plant Biologists
Issue Date: 2015
ISSN: 0032-0889
Statement of
Chuang Wang, Wenhao Yue, Yinghui Ying, Shoudong Wang, David Secco, Yu Liu, James Whelan, Stephen D. Tyerman, and Huixia Shou
Abstract: To maintain a stable cytosol phosphate (Pi) concentration, plant cells store Pi in their vacuoles. When the Pi concentration in the cytosol decreases, Pi is exported from the vacuole into the cytosol. This export is mediated by Pi transporters on the tonoplast. In this study, we demonstrate that SYG1, PHO81, and XPR1 (SPX)-Major Facility Superfamily (MFS) proteins have a similar structure with yeast (Saccharomyces cerevisiae) low-affinity Pi transporters Phosphatase87 (PHO87), PHO90, and PHO91. OsSPX-MFS1, OsSPX-MFS2, and OsSPX-MFS3 all localized on the tonoplast of rice (Oryza sativa) protoplasts, even in the absence of the SPX domain. At high external Pi concentration, OsSPX-MFS3 could partially complement the yeast mutant strain EY917 under pH 5.5, which lacks all five Pi transporters present in yeast. In oocytes, OsSPX-MFS3 was shown to facilitate Pi influx or efflux depending on the external pH and Pi concentrations. In contrast to tonoplast localization in plants cells, OsSPX-MFS3 was localized to the plasma membrane when expressed in both yeast and oocytes. Overexpression of OsSPX-MFS3 results in decreased Pi concentration in the vacuole of rice tissues. We conclude that OsSPX-MFS3 is a low-affinity Pi transporter that mediates Pi efflux from the vacuole into cytosol and is coupled to proton movement.
Keywords: Oocytes; Cell Membrane; Vacuoles; Cytosol; Protoplasts; Animals; Xenopus laevis; Phosphates; Phosphate Transport Proteins; Plant Proteins; Microscopy, Confocal; Gene Expression Profiling; Reverse Transcriptase Polymerase Chain Reaction; Gene Expression Regulation, Plant; Amino Acid Sequence; Sequence Homology, Amino Acid; Biological Transport; Homeostasis; Hydrogen-Ion Concentration; Molecular Sequence Data; Female; Oryza
Description: First Published on September 30, 2015
Rights: © 2015 American Society of Plant Biologists. All Rights Reserved.
RMID: 0030037149
DOI: 10.1104/pp.15.01005
Grant ID:
Appears in Collections:Agriculture, Food and Wine publications

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