Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure
Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also in...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Rodrigues, Olivier [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 114(2017), 34, Seite 9200 |
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| Übergeordnetes Werk: |
volume:114 ; year:2017 ; number:34 ; pages:9200 |
| Links: |
|---|
| DOI / URN: |
10.1073/pnas.1704754114 |
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| Katalog-ID: |
OLC1998534863 |
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| 245 | 1 | 0 | |a Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure |
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| 520 | |a Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. | ||
| 650 | 4 | |a Aquaporins | |
| 650 | 4 | |a Pretreatment | |
| 650 | 4 | |a Hydrogen ion concentration | |
| 650 | 4 | |a Plant protection | |
| 650 | 4 | |a Abscisic acid | |
| 650 | 4 | |a Studies | |
| 650 | 4 | |a Pathogens | |
| 650 | 4 | |a Guard cells | |
| 650 | 4 | |a Cell activation | |
| 650 | 4 | |a Kinases | |
| 650 | 4 | |a Permeability | |
| 650 | 4 | |a Stomata | |
| 650 | 4 | |a Phosphorylation | |
| 650 | 4 | |a Hydrogen peroxide | |
| 650 | 4 | |a Protoplasts | |
| 650 | 4 | |a Protein kinase | |
| 650 | 4 | |a Accumulation | |
| 650 | 4 | |a Phosphatidylinositol 4,5-diphosphate | |
| 700 | 1 | |a Reshetnyak, Ganna |4 oth | |
| 700 | 1 | |a Grondin, Alexandre |4 oth | |
| 700 | 1 | |a Saijo, Yusuke |4 oth | |
| 700 | 1 | |a Leonhardt, Nathalie |4 oth | |
| 700 | 1 | |a Maurel, Christophe |4 oth | |
| 700 | 1 | |a Verdoucq, Lionel |4 oth | |
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10.1073/pnas.1704754114 doi PQ20171228 (DE-627)OLC1998534863 (DE-599)GBVOLC1998534863 (PRQ)g1167-d4fd232c7ea13f0b453d4e26016bd2ce78119a8e27ec36b616534f5a40aed3250 (KEY)0583363920170000114003409200aquaporinsfacilitatehydrogenperoxideentryintoguard DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Rodrigues, Olivier verfasserin aut Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. Aquaporins Pretreatment Hydrogen ion concentration Plant protection Abscisic acid Studies Pathogens Guard cells Cell activation Kinases Permeability Stomata Phosphorylation Hydrogen peroxide Protoplasts Protein kinase Accumulation Phosphatidylinositol 4,5-diphosphate Reshetnyak, Ganna oth Grondin, Alexandre oth Saijo, Yusuke oth Leonhardt, Nathalie oth Maurel, Christophe oth Verdoucq, Lionel oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 34, Seite 9200 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:34 pages:9200 http://dx.doi.org/10.1073/pnas.1704754114 Volltext https://search.proquest.com/docview/1946431085 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 114 2017 34 9200 |
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10.1073/pnas.1704754114 doi PQ20171228 (DE-627)OLC1998534863 (DE-599)GBVOLC1998534863 (PRQ)g1167-d4fd232c7ea13f0b453d4e26016bd2ce78119a8e27ec36b616534f5a40aed3250 (KEY)0583363920170000114003409200aquaporinsfacilitatehydrogenperoxideentryintoguard DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Rodrigues, Olivier verfasserin aut Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. Aquaporins Pretreatment Hydrogen ion concentration Plant protection Abscisic acid Studies Pathogens Guard cells Cell activation Kinases Permeability Stomata Phosphorylation Hydrogen peroxide Protoplasts Protein kinase Accumulation Phosphatidylinositol 4,5-diphosphate Reshetnyak, Ganna oth Grondin, Alexandre oth Saijo, Yusuke oth Leonhardt, Nathalie oth Maurel, Christophe oth Verdoucq, Lionel oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 34, Seite 9200 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:34 pages:9200 http://dx.doi.org/10.1073/pnas.1704754114 Volltext https://search.proquest.com/docview/1946431085 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 114 2017 34 9200 |
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10.1073/pnas.1704754114 doi PQ20171228 (DE-627)OLC1998534863 (DE-599)GBVOLC1998534863 (PRQ)g1167-d4fd232c7ea13f0b453d4e26016bd2ce78119a8e27ec36b616534f5a40aed3250 (KEY)0583363920170000114003409200aquaporinsfacilitatehydrogenperoxideentryintoguard DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Rodrigues, Olivier verfasserin aut Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. Aquaporins Pretreatment Hydrogen ion concentration Plant protection Abscisic acid Studies Pathogens Guard cells Cell activation Kinases Permeability Stomata Phosphorylation Hydrogen peroxide Protoplasts Protein kinase Accumulation Phosphatidylinositol 4,5-diphosphate Reshetnyak, Ganna oth Grondin, Alexandre oth Saijo, Yusuke oth Leonhardt, Nathalie oth Maurel, Christophe oth Verdoucq, Lionel oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 34, Seite 9200 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:34 pages:9200 http://dx.doi.org/10.1073/pnas.1704754114 Volltext https://search.proquest.com/docview/1946431085 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 114 2017 34 9200 |
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10.1073/pnas.1704754114 doi PQ20171228 (DE-627)OLC1998534863 (DE-599)GBVOLC1998534863 (PRQ)g1167-d4fd232c7ea13f0b453d4e26016bd2ce78119a8e27ec36b616534f5a40aed3250 (KEY)0583363920170000114003409200aquaporinsfacilitatehydrogenperoxideentryintoguard DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Rodrigues, Olivier verfasserin aut Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. Aquaporins Pretreatment Hydrogen ion concentration Plant protection Abscisic acid Studies Pathogens Guard cells Cell activation Kinases Permeability Stomata Phosphorylation Hydrogen peroxide Protoplasts Protein kinase Accumulation Phosphatidylinositol 4,5-diphosphate Reshetnyak, Ganna oth Grondin, Alexandre oth Saijo, Yusuke oth Leonhardt, Nathalie oth Maurel, Christophe oth Verdoucq, Lionel oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 34, Seite 9200 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:34 pages:9200 http://dx.doi.org/10.1073/pnas.1704754114 Volltext https://search.proquest.com/docview/1946431085 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 114 2017 34 9200 |
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10.1073/pnas.1704754114 doi PQ20171228 (DE-627)OLC1998534863 (DE-599)GBVOLC1998534863 (PRQ)g1167-d4fd232c7ea13f0b453d4e26016bd2ce78119a8e27ec36b616534f5a40aed3250 (KEY)0583363920170000114003409200aquaporinsfacilitatehydrogenperoxideentryintoguard DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Rodrigues, Olivier verfasserin aut Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. Aquaporins Pretreatment Hydrogen ion concentration Plant protection Abscisic acid Studies Pathogens Guard cells Cell activation Kinases Permeability Stomata Phosphorylation Hydrogen peroxide Protoplasts Protein kinase Accumulation Phosphatidylinositol 4,5-diphosphate Reshetnyak, Ganna oth Grondin, Alexandre oth Saijo, Yusuke oth Leonhardt, Nathalie oth Maurel, Christophe oth Verdoucq, Lionel oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 34, Seite 9200 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:34 pages:9200 http://dx.doi.org/10.1073/pnas.1704754114 Volltext https://search.proquest.com/docview/1946431085 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 114 2017 34 9200 |
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Rodrigues, Olivier @@aut@@ Reshetnyak, Ganna @@oth@@ Grondin, Alexandre @@oth@@ Saijo, Yusuke @@oth@@ Leonhardt, Nathalie @@oth@@ Maurel, Christophe @@oth@@ Verdoucq, Lionel @@oth@@ |
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aquaporins facilitate hydrogen peroxide entry into guard cells to mediate aba- and pathogen-triggered stomatal closure |
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Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure |
| abstract |
Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. |
| abstractGer |
Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. |
| abstract_unstemmed |
Stomatal movements are crucial for the control of plant water status and protection against pathogens. Assays on epidermal peels revealed that, similar to abscisic acid (ABA), pathogen-associated molecular pattern (PAMP) flg22 requires the AtPIP2;1 aquaporin to induce stomatal closure. Flg22 also induced an increase in osmotic water permeability (Pf) of guard cell protoplasts through activation of AtPIP2;1. The use of HyPer, a genetic probe for intracellular hydrogen peroxide (H2O2), revealed that both ABA and flg22 triggered an accumulation of H2O2 in wild-type but not pip2;1 guard cells. Pretreatment of guard cells with flg22 or ABA facilitated the influx of exogenous H2O2. Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1) and open stomata 1 (OST1)/Snf1-related protein kinase 2.6 (SnRK2.6) were both necessary to flg22-induced Pf and both phosphorylated AtPIP2;1 on Ser121 in vitro. Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. This work establishes a signaling role of plasma membrane aquaporins in guard cells and potentially in other cellular context involving H2O2 signaling. |
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Accumulation of H2O2 and stomatal closure as induced by flg22 was restored in pip2;1 guard cells by a phosphomimetic form (Ser121Asp) but not by a phosphodeficient form (Ser121Ala) of AtPIP2;1. We propose a mechanism whereby phosphorylation of AtPIP2;1 Ser121 by BAK1 and/or OST1 is triggered in response to flg22 to activate its water and H2O2 transport activities. 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activation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Kinases</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Permeability</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Stomata</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Phosphorylation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Hydrogen peroxide</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protoplasts</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein kinase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Accumulation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Phosphatidylinositol 4,5-diphosphate</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Reshetnyak, Ganna</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Grondin, Alexandre</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Saijo, Yusuke</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Leonhardt, Nathalie</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Maurel, Christophe</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Verdoucq, Lionel</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Proceedings of the National Academy of Sciences of the United States of America</subfield><subfield code="d">Washington, DC : NAS, 1877</subfield><subfield code="g">114(2017), 34, Seite 9200</subfield><subfield code="w">(DE-627)129505269</subfield><subfield code="w">(DE-600)209104-5</subfield><subfield code="w">(DE-576)014909189</subfield><subfield code="x">0027-8424</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:114</subfield><subfield code="g">year:2017</subfield><subfield code="g">number:34</subfield><subfield code="g">pages:9200</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1073/pnas.1704754114</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">https://search.proquest.com/docview/1946431085</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-LING</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_59</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">114</subfield><subfield code="j">2017</subfield><subfield code="e">34</subfield><subfield code="h">9200</subfield></datafield></record></collection>
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