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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2006-2-20
pubmed:abstractText
ABI1 and ABI2 encode PP2C-type protein phosphatases and are thought to negatively regulate many aspects of abscisic acid (ABA) signaling, including stomatal closure in Arabidopsis. In contrast, SRK2E/OST1/SnRK2.6 encodes an Arabidopsis SnRK2 protein kinase and acts as a positive regulator in the ABA-induced stomatal closure. SRK2E/OST1 is activated by osmotic stress as well as by ABA, but the independence of the two activation processes has not yet been determined. Additionally, interaction between SRK2E/OST1 and PP2C-type phosphatases (ABI1 and ABI2) is not understood. In the present study, we demonstrated that the abi1-1 mutation, but not the abi2-1 mutation, strongly inhibited ABA-dependent SRK2E/OST1 activation. In contrast, osmotic stress activated SRK2E/OST1 even in abi1-1 and aba2-1 plants. The C-terminal regulatory domain of SRK2E/OST1 was required for its activation by both ABA and osmotic stress in Arabidopsis. The C-terminal domain was functionally divided into Domains I and II. Domain II was required only for the ABA-dependent activation of SRK2E/OST1, whereas Domain I was responsible for the ABA-independent activation. Full-length SRK2E/OST1 completely complemented the wilty phenotype of the srk2e mutant, but SRK2E/OST1 lacking Domain II did not. Domain II interacted with the ABI1 protein in a yeast two-hybrid assay. Our results suggested that the direct interaction between SRK2E/OST1 and ABI1 through Domain II plays a critical role in the control of stomatal closure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5310-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16365038-Abscisic Acid, pubmed-meshheading:16365038-Amino Acid Sequence, pubmed-meshheading:16365038-Arabidopsis, pubmed-meshheading:16365038-Arabidopsis Proteins, pubmed-meshheading:16365038-Gene Expression Regulation, Plant, pubmed-meshheading:16365038-Genes, Plant, pubmed-meshheading:16365038-Green Fluorescent Proteins, pubmed-meshheading:16365038-Models, Biological, pubmed-meshheading:16365038-Molecular Sequence Data, pubmed-meshheading:16365038-Mutation, pubmed-meshheading:16365038-Nitrate Reductase, pubmed-meshheading:16365038-Osmosis, pubmed-meshheading:16365038-Phenotype, pubmed-meshheading:16365038-Phosphoprotein Phosphatases, pubmed-meshheading:16365038-Plant Epidermis, pubmed-meshheading:16365038-Plant Growth Regulators, pubmed-meshheading:16365038-Plants, Genetically Modified, pubmed-meshheading:16365038-Protein Binding, pubmed-meshheading:16365038-Protein Kinases, pubmed-meshheading:16365038-Protein Structure, Tertiary, pubmed-meshheading:16365038-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:16365038-Sequence Homology, Amino Acid, pubmed-meshheading:16365038-Signal Transduction, pubmed-meshheading:16365038-Two-Hybrid System Techniques
pubmed:year
2006
pubmed:articleTitle
The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis.
pubmed:affiliation
Laboratory of Plant Molecular Biology, RIKEN Tsukuba Institute, 3-1-1, Koyadai, Tsukuba, Ibaraki 305-0074, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't