6533b853fe1ef96bd12ac102
RESEARCH PRODUCT
Evolution of osmosensing signal transduction in Metazoa: stress-activated protein kinases p38 and JNK.
Werner E.g. MüllerMarkus BöhmVera GamulinHeinz C. Schrödersubject
MAPK/ERK pathwayxHistologySaccharomyces cerevisiae ProteinsMAP Kinase Kinase 4p38 mitogen-activated protein kinasesSaccharomyces cerevisiaeMutantSaccharomyces cerevisiaeSodium Chloridep38 Mitogen-Activated Protein KinasesPathology and Forensic MedicineTransformation GeneticOsmotic PressureAnimalsMitogen-Activated Protein Kinase 8PhosphorylationProtein kinase APhylogenyMitogen-Activated Protein Kinase KinasesbiologyKinaseJNK Mitogen-Activated Protein KinasesCell BiologyWater-Electrolyte Balancebiology.organism_classificationCell biologyPoriferaPhosphorylationSignal transductionMitogen-Activated Protein KinasesSignal Transductiondescription
Sponges (Porifera) represent the most basal branch of the Metazoa alive today. We show that two central stress-activated protein kinases involved in the osmosensing pathway, p38 mitogen-activated protein kinase (MAPK) and JNK, can complement for the ancestral MAPK Hog1 in the yeast Saccharomyces cerevisiae. S. cerevisiae mutants lacking Hog1 (hog1-Delta 1) have been complemented with the sponge SDJNK and SDp38 genes. Western blotting has revealed that, after transformation, the hog1-Delta 1+ SDJNK(sense) and hog1-Delta 1+ SDp38(sense) clones express the sponge proteins. Functional studies have demonstrated that the complemented clones grow under hyperosmotic conditions (0.6 M NaCl). Furthermore, the expressed sponge kinases undergo phosphorylation in S. cerevisiae at 0.6 M NaCl. This report documents that the metazoan signal transduction kinases, p38 and JNK, which were originally derived from an common ancestor with yeast HOG1, have retained their function after their specification.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-08-22 | Cell and tissue research |