Elevated CO2 induces rapid dephosphorylation of plasma membrane H+‐ATPase in guard cells. Issue 6 (1st October 2022)
- Record Type:
- Journal Article
- Title:
- Elevated CO2 induces rapid dephosphorylation of plasma membrane H+‐ATPase in guard cells. Issue 6 (1st October 2022)
- Main Title:
- Elevated CO2 induces rapid dephosphorylation of plasma membrane H+‐ATPase in guard cells
- Authors:
- Ando, Eigo
Kollist, Hannes
Fukatsu, Kohei
Kinoshita, Toshinori
Terashima, Ichiro - Abstract:
- Summary: Light induces stomatal opening, which is driven by plasma membrane (PM) H + ‐ATPase in guard cells. The activation of guard‐cell PM H + ‐ATPase is mediated by phosphorylation of the penultimate C‐terminal residue, threonine. The phosphorylation is induced by photosynthesis as well as blue light photoreceptor phototropin. Here, we investigated the effects of cessation of photosynthesis on the phosphorylation level of guard‐cell PM H + ‐ATPase in Arabidopsis thaliana . Immunodetection of guard‐cell PM H + ‐ATPase, time‐resolved leaf gas‐exchange analyses and stomatal aperture measurements were carried out. We found that light–dark transition of leaves induced dephosphorylation of the penultimate residue at 1 min post‐transition. Gas‐exchange analyses confirmed that the dephosphorylation is accompanied by an increase in the intercellular CO2 concentration, caused by the cessation of photosynthetic CO2 fixation. We discovered that CO2 induces guard‐cell PM H + ‐ATPase dephosphorylation as well as stomatal closure. Interestingly, reverse‐genetic analyses using guard‐cell CO2 signal transduction mutants suggested that the dephosphorylation is mediated by a mechanism distinct from the established CO2 signalling pathway. Moreover, type 2C protein phosphatases D6 and D9 were required for the dephosphorylation and promoted stomatal closure upon the light–dark transition. Our results indicate that CO2 ‐mediated dephosphorylation of guard‐cell PM H + ‐ATPase underlies stomatalSummary: Light induces stomatal opening, which is driven by plasma membrane (PM) H + ‐ATPase in guard cells. The activation of guard‐cell PM H + ‐ATPase is mediated by phosphorylation of the penultimate C‐terminal residue, threonine. The phosphorylation is induced by photosynthesis as well as blue light photoreceptor phototropin. Here, we investigated the effects of cessation of photosynthesis on the phosphorylation level of guard‐cell PM H + ‐ATPase in Arabidopsis thaliana . Immunodetection of guard‐cell PM H + ‐ATPase, time‐resolved leaf gas‐exchange analyses and stomatal aperture measurements were carried out. We found that light–dark transition of leaves induced dephosphorylation of the penultimate residue at 1 min post‐transition. Gas‐exchange analyses confirmed that the dephosphorylation is accompanied by an increase in the intercellular CO2 concentration, caused by the cessation of photosynthetic CO2 fixation. We discovered that CO2 induces guard‐cell PM H + ‐ATPase dephosphorylation as well as stomatal closure. Interestingly, reverse‐genetic analyses using guard‐cell CO2 signal transduction mutants suggested that the dephosphorylation is mediated by a mechanism distinct from the established CO2 signalling pathway. Moreover, type 2C protein phosphatases D6 and D9 were required for the dephosphorylation and promoted stomatal closure upon the light–dark transition. Our results indicate that CO2 ‐mediated dephosphorylation of guard‐cell PM H + ‐ATPase underlies stomatal closure. … (more)
- Is Part Of:
- New phytologist. Volume 236:Issue 6(2022)
- Journal:
- New phytologist
- Issue:
- Volume 236:Issue 6(2022)
- Issue Display:
- Volume 236, Issue 6 (2022)
- Year:
- 2022
- Volume:
- 236
- Issue:
- 6
- Issue Sort Value:
- 2022-0236-0006-0000
- Page Start:
- 2061
- Page End:
- 2074
- Publication Date:
- 2022-10-01
- Subjects:
- Arabidopsis thaliana -- CO2 signalling -- dephosphorylation -- guard cell -- light–dark transition -- photosynthesis -- plasma membrane H+‐ATPase -- stomatal closure
Botany -- Periodicals
580 - Journal URLs:
- http://nph.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1469-8137/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/nph.18472 ↗
- Languages:
- English
- ISSNs:
- 0028-646X
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6085.000000
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