Reference - Detail
|Author||Ott A, Oehme F, Keller H, Schuster SC.|
|Title||Osmotic stress response in Dictyostelium is mediated by cAMP.|
DokA, a homolog of bacterial hybrid histidine kinases, is essential for hyperosmotic stress resistance in Dictyostelium: We show that a transient intracellular cAMP signal, dependent on the presence of DokA, is generated in response to an osmotic shock. This variation of cAMP levels contributes to survival under hypertonic conditions. In contrast to the low cAMP levels observed in dokA(-) strains, overexpression of the receiver domain of DokA causes an increase in cAMP levels, resulting in a rapidly developing phenotype. We present biochemical and cell biological data indicating that the DokA receiver domain is a dominant-negative regulator of a phosphorelay, which controls the intracellular cAMP phosphodiesterase RegA. The activity of the DokA receiver domain depends on a conserved aspartate, mutation of which reverses the developmental phenotype, as well as the deregulation of cAMP metabolism.
|MeSH||3',5'-Cyclic-AMP Phosphodiesterases 8-Bromo Cyclic Adenosine Monophosphate / pharmacology Animals Cyclic AMP / metabolism* Cyclic AMP-Dependent Protein Kinases / metabolism DNA-Binding Proteins / metabolism Dictyostelium / genetics Dictyostelium / growth & development Dictyostelium / metabolism* Gene Expression Osmotic Pressure Phenotype Protein Kinases / chemistry Protein Kinases / genetics Protein Kinases / metabolism Protein Structure, Tertiary Protozoan Proteins / metabolism Signal Transduction|
|WOS Category||BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY|
|Cellular slime molds||G24199|