Your browser doesn't support javascript.
loading
A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis.
Liu, Jinlong; Yang, Lei; Luan, Mingda; Wang, Yuan; Zhang, Chi; Zhang, Bin; Shi, Jisen; Zhao, Fu-Geng; Lan, Wenzhi; Luan, Sheng.
Afiliação
  • Liu J; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China;
  • Yang L; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China;
  • Luan M; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China;
  • Wang Y; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China;
  • Zhang C; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China;
  • Zhang B; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China;
  • Shi J; Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, Key Laboratory of Forest Genetics and Biotechnology, Nanjing Forestry University, Nanjing 210037, China;
  • Zhao FG; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China; fgzhao@nju.edu.cn lanw@nju.edu.cn sluan@berkeley.edu.
  • Lan W; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China; fgzhao@nju.edu.cn lanw@nju.edu.cn sluan@berkeley.edu.
  • Luan S; State Key Laboratory for Pharmaceutical Biotechnology, Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China; Department of Plant and Microbial Biology, University of California, Berkeley, CA 94
Proc Natl Acad Sci U S A ; 112(47): E6571-8, 2015 Nov 24.
Article em En | MEDLINE | ID: mdl-26554016
Inorganic phosphate (Pi) is stored in the vacuole, allowing plants to adapt to variable Pi availability in the soil. The transporters that mediate Pi sequestration into vacuole remain unknown, however. Here we report the functional characterization of Vacuolar Phosphate Transporter 1 (VPT1), an SPX domain protein that transports Pi into the vacuole in Arabidopsis. The vpt1 mutant plants were stunted and consistently retained less Pi than wild type plants, especially when grown in medium containing high levels of Pi. In seedlings, VPT1 was expressed primarily in younger tissues under normal conditions, but was strongly induced by high-Pi conditions in older tissues, suggesting that VPT1 functions in Pi storage in young tissues and in detoxification of high Pi in older tissues. As a result, disruption of VPT1 rendered plants hypersensitive to both low-Pi and high-Pi conditions, reducing the adaptability of plants to changing Pi availability. Patch-clamp analysis of isolated vacuoles showed that the Pi influx current was severely reduced in vpt1 compared with wild type plants. When ectopically expressed in Nicotiana benthamiana mesophyll cells, VPT1 mediates vacuolar influx of anions, including Pi, SO4(2-), NO3(-), Cl(-), and malate with Pi as that preferred anion. The VPT1-mediated Pi current amplitude was dependent on cytosolic phosphate concentration. Single-channel analysis showed that the open probability of VPT1 was increased with the increase in transtonoplast potential. We conclude that VPT1 is a transporter responsible for vacuolar Pi storage and is essential for Pi adaptation in Arabidopsis.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfatos / Vacúolos / Arabidopsis / Proteínas de Transporte de Fosfato / Proteínas de Arabidopsis / Homeostase Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfatos / Vacúolos / Arabidopsis / Proteínas de Transporte de Fosfato / Proteínas de Arabidopsis / Homeostase Idioma: En Ano de publicação: 2015 Tipo de documento: Article