The plant hormone abscisic acid (ABA) mediates various responses such as stomatal closure, the maintenance of seed dormancy, and the inhibition of plant growth. All three responses are affected in the ABA-insensitive mutant abi1 of Arabidopsis thaliana, suggesting that an early step in the signaling of ABA is controlled by the ABI1 locus. The ABI1 gene was cloned by chromosome walking, and a missense mutation was identified in the structural gene of the abi1 mutant. The ABI1 gene encodes a protein with high similarity to protein serine or threonine phosphatases of type 2C with the novel feature of a putative Ca2+ binding site. Thus, the control of the phosphorylation state of cell signaling components by the ABI1 product could mediate pleiotropic hormone responses.

ABI1, a protein phosphatase 2C, is a key component of signal transduction in Arabidopsis. It regulates diverse responses to the phytohormone abscisic acid (ABA) such as stomatal closure, seed dormancy and inhibition of vegetative growth. By analysing proteins capable of interacting with ABI1, we have identified the homeodomain protein ATHB6 as a regulator of the ABA signal pathway. Critical for interaction between ATHB6 and ABI1 is an intact protein phosphatase domain and the N‐terminal domain of ATHB6 containing the DNA‐binding site. ATHB6 recognizes a cis‐element present in its promoter, which encompasses the core motif (CAATTATTA) that mediated ATHB6‐ and ABA‐dependent gene expression in protoplasts. In addition, transgenic plants containing a luciferase gene controlled by the ATHB6 promoter documented a strong ABA‐inducible expression of the reporter which was abrogated in the ABA‐insensitive abi1 mutant. Arabidopsis plants with constitutive expression of the transcriptional regulator revealed ABA insensitivity in a subset of ABI1‐dependent responses. Thus, the homeodomain protein ATHB6 seems to represent a negative regulator of the ABA signal pathway and to act downstream of ABI1.

The regulation of intracellular ion concentrations is a fundamental property of living cells. Although many ion transporters have been identified, the systems that modulate their activity remain largely unknown. We have characterized two partially redundant genes from Saccharomyces cerevisiae, HAL4/SAT4 and HAL5, that encode homologous protein kinases implicated in the regulation of cation uptake. Overexpression of these genes increases the tolerance of yeast cells to sodium and lithium, whereas gene disruptions result in greater cation sensitivity. These phenotypic effects of the mutations correlate with changes in cation uptake and are dependent on a functional Trk1-Trk2 potassium transport system. In addition, hal4 hal5 and trk1 trk2 mutants exhibit similar phenotypes: (i) they are deficient in potassium uptake; (ii) their growth is sensitive to a variety of toxic cations, including lithium, sodium, calcium, tetramethylammonium, hygromycin B, and low pH; and (iii) they exhibit increased uptake of methylammonium, an indicator of membrane potential. These results suggest that the Hal4 and Hal5 protein kinases activate the Trk1-Trk2 potassium transporter, increasing the influx of potassium and decreasing the membrane potential. The resulting loss in electrical driving force reduces the uptake of toxic cations and improves salt tolerance. Our data support a role for regulation of membrane potential in adaptation to salt stress that is mediated by the Hal4 and Hal5 kinases.

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