A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis

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...
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Autor*in:	Jisen Shi [verfasserIn] Yuan Wang Wenzhi Lan Bin Zhang Lei Yang Chi Zhang Jinlong Liu Mingda Luan Sheng Luan Fu-Geng Zhao

Format:	Artikel
Sprache:	Englisch

Erschienen:	2015

Rechteinformationen:	Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences

Schlagwörter:	Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells

Übergeordnetes Werk:	Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 112(2015), 47, Seite E6571
Übergeordnetes Werk:	volume:112 ; year:2015 ; number:47 ; pages:E6571

Links:	Volltext Link aufrufen Link aufrufen Link aufrufen

DOI / URN:	10.1073/pnas.1514598112

Katalog-ID:	OLC1970292695

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245	1	2	\|a A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis
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520			\|a 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.
540			\|a Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences
650		4	\|a Observations
650		4	\|a Homeostasis
650		4	\|a Arabidopsis thaliana
650		4	\|a Carrier proteins
650		4	\|a Physiological aspects
650		4	\|a Tissue
650		4	\|a Flowers & plants
650		4	\|a Proteins
650		4	\|a Phosphates
650		4	\|a Cells
700	0		\|a Yuan Wang \|4 oth
700	0		\|a Wenzhi Lan \|4 oth
700	0		\|a Bin Zhang \|4 oth
700	0		\|a Lei Yang \|4 oth
700	0		\|a Chi Zhang \|4 oth
700	0		\|a Jinlong Liu \|4 oth
700	0		\|a Mingda Luan \|4 oth
700	0		\|a Sheng Luan \|4 oth
700	0		\|a Fu-Geng Zhao \|4 oth
773	0	8	\|i Enthalten in \|t Proceedings of the National Academy of Sciences of the United States of America \|d Washington, DC : NAS, 1877 \|g 112(2015), 47, Seite E6571 \|w (DE-627)129505269 \|w (DE-600)209104-5 \|w (DE-576)014909189 \|x 0027-8424 \|7 nnns
773	1	8	\|g volume:112 \|g year:2015 \|g number:47 \|g pages:E6571
856	4	1	\|u http://dx.doi.org/10.1073/pnas.1514598112 \|3 Volltext
856	4	2	\|u http://www.pnas.org/content/112/47/E6571.abstract
856	4	2	\|u http://www.ncbi.nlm.nih.gov/pubmed/26554016
856	4	2	\|u http://search.proquest.com/docview/1739096714
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allfields	10.1073/pnas.1514598112 doi PQ20160211 (DE-627)OLC1970292695 (DE-599)GBVOLC1970292695 (PRQ)g1582-425959f859ad763512ebbb24289543c3922077df3d0782406179486ef03db98c0 (KEY)0583363920150000112004706571vacuolarphosphatetransporteressentialforphosphateh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Jisen Shi verfasserin aut A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells Yuan Wang oth Wenzhi Lan oth Bin Zhang oth Lei Yang oth Chi Zhang oth Jinlong Liu oth Mingda Luan oth Sheng Luan oth Fu-Geng Zhao oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 47, Seite E6571 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:47 pages:E6571 http://dx.doi.org/10.1073/pnas.1514598112 Volltext http://www.pnas.org/content/112/47/E6571.abstract http://www.ncbi.nlm.nih.gov/pubmed/26554016 http://search.proquest.com/docview/1739096714 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 47 E6571
spelling	10.1073/pnas.1514598112 doi PQ20160211 (DE-627)OLC1970292695 (DE-599)GBVOLC1970292695 (PRQ)g1582-425959f859ad763512ebbb24289543c3922077df3d0782406179486ef03db98c0 (KEY)0583363920150000112004706571vacuolarphosphatetransporteressentialforphosphateh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Jisen Shi verfasserin aut A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells Yuan Wang oth Wenzhi Lan oth Bin Zhang oth Lei Yang oth Chi Zhang oth Jinlong Liu oth Mingda Luan oth Sheng Luan oth Fu-Geng Zhao oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 47, Seite E6571 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:47 pages:E6571 http://dx.doi.org/10.1073/pnas.1514598112 Volltext http://www.pnas.org/content/112/47/E6571.abstract http://www.ncbi.nlm.nih.gov/pubmed/26554016 http://search.proquest.com/docview/1739096714 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 47 E6571
allfields_unstemmed	10.1073/pnas.1514598112 doi PQ20160211 (DE-627)OLC1970292695 (DE-599)GBVOLC1970292695 (PRQ)g1582-425959f859ad763512ebbb24289543c3922077df3d0782406179486ef03db98c0 (KEY)0583363920150000112004706571vacuolarphosphatetransporteressentialforphosphateh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Jisen Shi verfasserin aut A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells Yuan Wang oth Wenzhi Lan oth Bin Zhang oth Lei Yang oth Chi Zhang oth Jinlong Liu oth Mingda Luan oth Sheng Luan oth Fu-Geng Zhao oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 47, Seite E6571 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:47 pages:E6571 http://dx.doi.org/10.1073/pnas.1514598112 Volltext http://www.pnas.org/content/112/47/E6571.abstract http://www.ncbi.nlm.nih.gov/pubmed/26554016 http://search.proquest.com/docview/1739096714 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 47 E6571
allfieldsGer	10.1073/pnas.1514598112 doi PQ20160211 (DE-627)OLC1970292695 (DE-599)GBVOLC1970292695 (PRQ)g1582-425959f859ad763512ebbb24289543c3922077df3d0782406179486ef03db98c0 (KEY)0583363920150000112004706571vacuolarphosphatetransporteressentialforphosphateh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Jisen Shi verfasserin aut A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells Yuan Wang oth Wenzhi Lan oth Bin Zhang oth Lei Yang oth Chi Zhang oth Jinlong Liu oth Mingda Luan oth Sheng Luan oth Fu-Geng Zhao oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 47, Seite E6571 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:47 pages:E6571 http://dx.doi.org/10.1073/pnas.1514598112 Volltext http://www.pnas.org/content/112/47/E6571.abstract http://www.ncbi.nlm.nih.gov/pubmed/26554016 http://search.proquest.com/docview/1739096714 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 47 E6571
allfieldsSound	10.1073/pnas.1514598112 doi PQ20160211 (DE-627)OLC1970292695 (DE-599)GBVOLC1970292695 (PRQ)g1582-425959f859ad763512ebbb24289543c3922077df3d0782406179486ef03db98c0 (KEY)0583363920150000112004706571vacuolarphosphatetransporteressentialforphosphateh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Jisen Shi verfasserin aut A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells Yuan Wang oth Wenzhi Lan oth Bin Zhang oth Lei Yang oth Chi Zhang oth Jinlong Liu oth Mingda Luan oth Sheng Luan oth Fu-Geng Zhao oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 47, Seite E6571 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:47 pages:E6571 http://dx.doi.org/10.1073/pnas.1514598112 Volltext http://www.pnas.org/content/112/47/E6571.abstract http://www.ncbi.nlm.nih.gov/pubmed/26554016 http://search.proquest.com/docview/1739096714 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 47 E6571
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author	Jisen Shi
spellingShingle	Jisen Shi ddc 500 ddc 570 fid LING fid BIODIV misc Observations misc Homeostasis misc Arabidopsis thaliana misc Carrier proteins misc Physiological aspects misc Tissue misc Flowers & plants misc Proteins misc Phosphates misc Cells A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis
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topic_title	500 DNB 570 AVZ LING fid BIODIV fid A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis Observations Homeostasis Arabidopsis thaliana Carrier proteins Physiological aspects Tissue Flowers & plants Proteins Phosphates Cells
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title	A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis
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title_full	A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis
author_sort	Jisen Shi
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title_sort	vacuolar phosphate transporter essential for phosphate homeostasis in arabidopsis
title_auth	A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis
abstract	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.
abstractGer	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.
abstract_unstemmed	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.
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container_issue	47
title_short	A vacuolar phosphate transporter essential for phosphate homeostasis in Arabidopsis
url	http://dx.doi.org/10.1073/pnas.1514598112 http://www.pnas.org/content/112/47/E6571.abstract http://www.ncbi.nlm.nih.gov/pubmed/26554016 http://search.proquest.com/docview/1739096714
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author2	Yuan Wang Wenzhi Lan Bin Zhang Lei Yang Chi Zhang Jinlong Liu Mingda Luan Sheng Luan Fu-Geng Zhao
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up_date	2024-07-03T14:41:43.979Z
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