Reversible phosphorylation of histidine residues in proteins from vertebrates.
Signaling by kinases and phosphatases that act on serine, threonine, and tyrosine residues of proteins is among the most extensively studied regulatory mechanisms in mammalian cells, and research focused in this area is ongoing. We are just beginning to appreciate that such signaling mechanisms are extended and enriched by the reversible phosphorylation of histidine residues. The most exciting developments in this field to date come from studies on the beta subunit of heterotrimeric guanosine triphosphate-binding proteins (G proteins), the enzyme adenosine 5'-triphosphate-citrate lyase, and now the Ca(2+)-activated K(+) channel KCa3.1, all of which are targeted by nucleoside diphosphate kinase (which phosphorylates histidines) and protein histidine phosphatase (which dephosphorylates phosphorylated histidines).
Klumpp
Susanne
S
Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität, D-48149 Münster, Germany. k.secretary@uni-muenster.de
Krieglstein
Josef
J
D000818:Animals; D019204:GTP-Binding Proteins / Q000378:metabolism; D006639:Histidine / Q000378:metabolism*; D006801:Humans; D051660:Intermediate-Conductance Calcium-Activated Potassium Channels / Q000378:metabolism; D008954:Models, Biological; D009701:Nucleoside-Diphosphate Kinase / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D015398:Signal Transduction / Q000502:physiology*; D014714:Vertebrates
D051660:Intermediate-Conductance Calcium-Activated Potassium Channels; C496923:KCNN4 protein, human; D006639:Histidine; D009701:Nucleoside-Diphosphate Kinase; C504019:PHPT1 protein, human; D010744:Phosphoric Monoester Hydrolases; D019204:GTP-Binding Proteins