Article
Phosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway.
Molecular and cellular biology - 1 Sept 2008
Horie Tetsuro, Tatebayashi Kazuo, Yamada Rika, Saito Haruo
Abstract excerpt
In Saccharomyces cerevisiae, external high osmolarity activates the Hog1 mitogen-activated protein kinase (MAPK), which controls various aspects of osmoadaptation. Ssk1 is a homolog of bacterial two-component response regulators and activates the Ssk2 MAPK kinase kinase upstream of Hog1. It has been proposed that unphosphorylated Ssk1 (Ssk1-OH) is the active form and that Ssk1 phosphorylated (Ssk1 approximately...
Topics
- Amino Acid Substitution
- Aspartic Acid
- Dimerization
- Enzyme Activation
- Genes, Dominant
- Glycerol
- MAP Kinase Kinase Kinases
- Models, Biological
- Mutation
- Osmolar Concentration