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CPK13, a noncanonical Ca2+-dependent protein kinase, specifically inhibits KAT2 and KAT1 shaker K+ channels and reduces stomatal opening.
- Source :
-
Plant physiology [Plant Physiol] 2014 Sep; Vol. 166 (1), pp. 314-26. Date of Electronic Publication: 2014 Jul 18. - Publication Year :
- 2014
-
Abstract
- Ca(2) (+)-dependent protein kinases (CPKs) form a large family of 34 genes in Arabidopsis (Arabidopsis thaliana). Based on their dependence on Ca(2+), CPKs can be sorted into three types: strictly Ca(2+)-dependent CPKs, Ca(2+)-stimulated CPKs (with a significant basal activity in the absence of Ca(2+)), and essentially calcium-insensitive CPKs. Here, we report on the third type of CPK, CPK13, which is expressed in guard cells but whose role is still unknown. We confirm the expression of CPK13 in Arabidopsis guard cells, and we show that its overexpression inhibits light-induced stomatal opening. We combine several approaches to identify a guard cell-expressed target. We provide evidence that CPK13 (1) specifically phosphorylates peptide arrays featuring Arabidopsis K(+) Channel KAT2 and KAT1 polypeptides, (2) inhibits KAT2 and/or KAT1 when expressed in Xenopus laevis oocytes, and (3) closely interacts in plant cells with KAT2 channels (Förster resonance energy transfer-fluorescence lifetime imaging microscopy). We propose that CPK13 reduces stomatal aperture through its inhibition of the guard cell-expressed KAT2 and KAT1 channels.<br /> (© 2014 American Society of Plant Biologists. All Rights Reserved.)
- Subjects :
- Animals
Calcium metabolism
Microscopy, Fluorescence
Patch-Clamp Techniques
Phosphorylation
Xenopus laevis
Arabidopsis enzymology
Arabidopsis Proteins metabolism
Plant Stomata enzymology
Potassium Channels, Inwardly Rectifying metabolism
Potassium Channels, Voltage-Gated metabolism
Protein Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1532-2548
- Volume :
- 166
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Plant physiology
- Publication Type :
- Academic Journal
- Accession number :
- 25037208
- Full Text :
- https://doi.org/10.1104/pp.114.240226