Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening
Abstract Plasma membrane (PM) H+-ATPase is crucial for light-induced stomatal opening and phosphorylation of a penultimate residue, Thr948 (pen-Thr, numbering according to Arabidopsis AHA1) is required for enzyme activation. In this study, a comprehensive phosphoproteomic analysis using guard cell p...
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| Format: | Article |
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Nature Portfolio
2024-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-45248-5 |
| _version_ | 1797274024413233152 |
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| author | Yuki Hayashi Kohei Fukatsu Koji Takahashi Satoru N. Kinoshita Kyohei Kato Taku Sakakibara Keiko Kuwata Toshinori Kinoshita |
| author_facet | Yuki Hayashi Kohei Fukatsu Koji Takahashi Satoru N. Kinoshita Kyohei Kato Taku Sakakibara Keiko Kuwata Toshinori Kinoshita |
| author_sort | Yuki Hayashi |
| collection | DOAJ |
| description | Abstract Plasma membrane (PM) H+-ATPase is crucial for light-induced stomatal opening and phosphorylation of a penultimate residue, Thr948 (pen-Thr, numbering according to Arabidopsis AHA1) is required for enzyme activation. In this study, a comprehensive phosphoproteomic analysis using guard cell protoplasts from Vicia faba shows that both red and blue light increase the phosphorylation of Thr881, of PM H+-ATPase. Light-induced stomatal opening and the blue light-induced increase in stomatal conductance are reduced in transgenic Arabidopsis plants expressing mutant AHA1-T881A in aha1–9, whereas the blue light-induced phosphorylation of pen-Thr is unaffected. Auxin and photosynthetically active radiation induce the phosphorylation of both Thr881 and pen-Thr in etiolated seedlings and leaves, respectively. The dephosphorylation of phosphorylated Thr881 and pen-Thr are mediated by type 2 C protein phosphatase clade D isoforms. Taken together, Thr881 phosphorylation, in addition of the pen-Thr phosphorylation, are important for PM H+-ATPase function during physiological responses, such as light-induced stomatal opening in Arabidopsis thaliana. |
| first_indexed | 2024-03-07T14:52:29Z |
| format | Article |
| id | doaj.art-531d292c90d445fdb4c8fcc4e93b7b5f |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-07T14:52:29Z |
| publishDate | 2024-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-531d292c90d445fdb4c8fcc4e93b7b5f2024-03-05T19:36:08ZengNature PortfolioNature Communications2041-17232024-02-0115111210.1038/s41467-024-45248-5Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal openingYuki Hayashi0Kohei Fukatsu1Koji Takahashi2Satoru N. Kinoshita3Kyohei Kato4Taku Sakakibara5Keiko Kuwata6Toshinori Kinoshita7Graduate School of Science, Nagoya UniversityGraduate School of Science, Nagoya UniversityGraduate School of Science, Nagoya UniversityGraduate School of Science, Nagoya UniversityGraduate School of Science, Nagoya UniversityGraduate School of Science, Nagoya UniversityInstitute of Transformative Bio-Molecules (WPI-ITbM), Nagoya UniversityGraduate School of Science, Nagoya UniversityAbstract Plasma membrane (PM) H+-ATPase is crucial for light-induced stomatal opening and phosphorylation of a penultimate residue, Thr948 (pen-Thr, numbering according to Arabidopsis AHA1) is required for enzyme activation. In this study, a comprehensive phosphoproteomic analysis using guard cell protoplasts from Vicia faba shows that both red and blue light increase the phosphorylation of Thr881, of PM H+-ATPase. Light-induced stomatal opening and the blue light-induced increase in stomatal conductance are reduced in transgenic Arabidopsis plants expressing mutant AHA1-T881A in aha1–9, whereas the blue light-induced phosphorylation of pen-Thr is unaffected. Auxin and photosynthetically active radiation induce the phosphorylation of both Thr881 and pen-Thr in etiolated seedlings and leaves, respectively. The dephosphorylation of phosphorylated Thr881 and pen-Thr are mediated by type 2 C protein phosphatase clade D isoforms. Taken together, Thr881 phosphorylation, in addition of the pen-Thr phosphorylation, are important for PM H+-ATPase function during physiological responses, such as light-induced stomatal opening in Arabidopsis thaliana.https://doi.org/10.1038/s41467-024-45248-5 |
| spellingShingle | Yuki Hayashi Kohei Fukatsu Koji Takahashi Satoru N. Kinoshita Kyohei Kato Taku Sakakibara Keiko Kuwata Toshinori Kinoshita Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening Nature Communications |
| title | Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening |
| title_full | Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening |
| title_fullStr | Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening |
| title_full_unstemmed | Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening |
| title_short | Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening |
| title_sort | phosphorylation of plasma membrane h atpase thr881 participates in light induced stomatal opening |
| url | https://doi.org/10.1038/s41467-024-45248-5 |
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