title: The role of ABI1 in abscisic acid signal transduction: from gene to cell.
abstract: The semi-dominant abi1-1 mutation of Arabidopsis interferes with multiple aspects of abscisic acid signal transduction resulting in reduced seed dormancy and sensitivity of root growth in ABA. Furthermore, the mutant transpires excessively as a result of abnormal stomatal regulation leading to a wilty phenotype. The ABI1 gene has been cloned. The carboxyl-terminal domain of the predicted ABI1 protein is related to the 2C class of serine-threonine phosphatases while no overt homology was found in the extended amino terminus. A combination of in vitro assays and yeast mutant complementation studies confirmed that ABI1 is a functional protein phosphatase 2C. The abi1-1 mutation converts the amino acid glycine180 to aspartic acid, and in the above test systems, causes a partial loss of the phosphatase activity. In transgenic Nicotiana benthamiana guard cells, the abi1-1 gene causes a reduction in the background current of the outward-rectifying potassium channels, and also in the abscisic acid-sensitivity of both the outward- and the inward-rectifying potassium channels in the plasma membrane. However, normal sensitivity of both potassium channels to, and stomatal closure in, abscisic acid was recovered in the presence of H7 and staurosporine, both broad-range protein kinase antagonists. These results suggest the aberrant potassium channel behavior as a major consequence of abi1-1 action and implicate ABI1 as part of a phosphatase/kinase pathway that modulates the sensitivity of guard-cell potassium channels to abscisic acid-evoked signal cascades.
authors.affiliation: Institut des Sciences Végétales, Centre National de la Recherche Scientifique UPR 40, Gif-sur-Yvette, France.
authors.forename: J
authors.initials: J
authors.lastname: Leung
authors.forename: S
authors.initials: S
authors.lastname: Merlot
authors.forename: F
authors.initials: F
authors.lastname: Gosti
authors.forename: N
authors.initials: N
authors.lastname: Bertauche
authors.forename: M R
authors.initials: MR
authors.lastname: Blatt
authors.forename: J
authors.initials: J
authors.lastname: Giraudat
mesh_terms: D000040:Abscisic Acid / Q000378:metabolism*; D029681:Arabidopsis Proteins; D003001:Cloning, Molecular; D004791:Enzyme Inhibitors / Q000494:pharmacology; D017343:Genes, Plant; D009154:Mutation; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D030821:Plants, Genetically Modified; D010947:Plants, Toxic; D015221:Potassium Channels / Q000187:drug effects / Q000378:metabolism*; D011493:Protein Kinase C / Q000037:antagonists & inhibitors; D015398:Signal Transduction / Q000235:genetics*; D019311:Staurosporine / Q000494:pharmacology; D014026:Nicotiana
chemical_list: D029681:Arabidopsis Proteins; D004791:Enzyme Inhibitors; D015221:Potassium Channels; D000040:Abscisic Acid; D011493:Protein Kinase C; C087434:ABI1 protein, Arabidopsis; D010749:Phosphoprotein Phosphatases; D019311:Staurosporine