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• W2480157777 abstract "Phosphorelay from histidine kinases to response regulators controls a myriad of processes in bacteria but appears to be more specialized in eukaryotes. At least 15 members of the histidine kinase family can be recognized in the genomic sequences of Dictyostelium discoideum. The predicted products of each of these genes have well-conserved catalytic and receiver domains. One member of the family, DhkD, is a double histidine kinase with two catalytic and two receiver domains. Alignment of this large family with the Sln1 histidine kinase of yeast extends the sequence profile that characterizes eukaryotic histidine kinases. DhkA is a transmembrane receptor kinase that autophosphorylates and relays the phosphate to the receiver aspartate when dimerized. Genetic studies on dhkA, dhkB, dhkC, and dokA have indicated their roles in cellular and developmental processes. It is likely that DhkC relays phosphate to the N-terminal receiver domain of the cAMP phosphodiesterase RegA through the H2 domain of RdeA. DhkA and DhkB appear to inhibit RegA activity by indirectly activating the MAP kinase ERK2. When the carboxy-terminal region of RegA is phosphorylated, phosphodiesterase activity is inhibited. Histidine kinases may also activate the late adenylyl kinase, ACR. Thus, these histidine kinases seem to be focused on regulating cAMP to modulate the activity of the cAMP-dependent protein kinase, PKA." @default.
• W2480157777 created "2016-08-23" @default.
• W2480157777 creator A5014612742 @default.
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• W2480157777 date "2003-01-01" @default.
• W2480157777 modified "2023-09-25" @default.
• W2480157777 title "Histidine Kinases of Dictyostelium" @default.
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• W2480157777 doi "https://doi.org/10.1016/b978-012372484-7/50021-7" @default.
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