Open stomata 1 (OST1) kinase controls R–type anion channel QUAC1 in Arabidopsis guard cells. (22nd March 2013)
- Record Type:
- Journal Article
- Title:
- Open stomata 1 (OST1) kinase controls R–type anion channel QUAC1 in Arabidopsis guard cells. (22nd March 2013)
- Main Title:
- Open stomata 1 (OST1) kinase controls R–type anion channel QUAC1 in Arabidopsis guard cells
- Authors:
- Imes, Dennis
Mumm, Patrick
Böhm, Jennifer
Al‐Rasheid, Khaled A. S.
Marten, Irene
Geiger, Dietmar
Hedrich, Rainer - Abstract:
- <abstract abstract-type="main" id="tpj12133-abs-0001"> <title>Summary</title> <p>Under drought stress, the stress hormone ABA addresses the SnR kinase OST1 via its cytosolic receptor and the protein phosphatase ABI1. Upon activation, OST1 phosphorylates the guard cell S–type anion channel SLAC1. Arabidopsis ABI1 and OST1 loss‐of‐function mutants are characterized by an extreme wilting 'open stomata′ phenotype. Given the fact that guard cells express both SLAC‐ and R–/QUAC‐type anion channels, we questioned whether OST1, besides SLAC1, also controls the QUAC1 channel. In other words, are ABI1/OST1 defects preventing both of the guard cell anion channel types from operating properly in terms of stomatal closure? The activation of the R–/QUAC‐type anion channel by ABA signaling kinase OST1 and phosphatase ABI1 was analyzed in two experimental systems: Arabidopsis guard cells and the plant cell‐free background of <italic>Xenopus oocytes</italic>. Patch‐clamp studies on guard cells show that ABA activates R–/QUAC‐type currents of wild‐type plants, but to a much lesser extent in those of <italic>abi1–1</italic> and <italic>ost1–2</italic> mutants. In the oocyte system the co‐expression of QUAC1 and OST1 resulted in a pronounced activation of the R–type anion channel. These studies indicate that OST1 is addressing both S–/SLAC‐ and R–/QUAC‐type guard cell anion channels, and explain why the <italic>ost1–2</italic> mutant is much more sensitive to drought than single<abstract abstract-type="main" id="tpj12133-abs-0001"> <title>Summary</title> <p>Under drought stress, the stress hormone ABA addresses the SnR kinase OST1 via its cytosolic receptor and the protein phosphatase ABI1. Upon activation, OST1 phosphorylates the guard cell S–type anion channel SLAC1. Arabidopsis ABI1 and OST1 loss‐of‐function mutants are characterized by an extreme wilting 'open stomata′ phenotype. Given the fact that guard cells express both SLAC‐ and R–/QUAC‐type anion channels, we questioned whether OST1, besides SLAC1, also controls the QUAC1 channel. In other words, are ABI1/OST1 defects preventing both of the guard cell anion channel types from operating properly in terms of stomatal closure? The activation of the R–/QUAC‐type anion channel by ABA signaling kinase OST1 and phosphatase ABI1 was analyzed in two experimental systems: Arabidopsis guard cells and the plant cell‐free background of <italic>Xenopus oocytes</italic>. Patch‐clamp studies on guard cells show that ABA activates R–/QUAC‐type currents of wild‐type plants, but to a much lesser extent in those of <italic>abi1–1</italic> and <italic>ost1–2</italic> mutants. In the oocyte system the co‐expression of QUAC1 and OST1 resulted in a pronounced activation of the R–type anion channel. These studies indicate that OST1 is addressing both S–/SLAC‐ and R–/QUAC‐type guard cell anion channels, and explain why the <italic>ost1–2</italic> mutant is much more sensitive to drought than single <italic>slac1</italic> or <italic>quac1</italic> mutants.</p> </abstract> … (more)
- Is Part Of:
- Plant journal. Volume 74:Number 3(2013:May)
- Journal:
- Plant journal
- Issue:
- Volume 74:Number 3(2013:May)
- Issue Display:
- Volume 74, Issue 3 (2013)
- Year:
- 2013
- Volume:
- 74
- Issue:
- 3
- Issue Sort Value:
- 2013-0074-0003-0000
- Page Start:
- 372
- Page End:
- 382
- Publication Date:
- 2013-03-22
- Subjects:
- Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.12133 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3773.xml