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Sci. Signal., 10 March 2009
Vol. 2, Issue 61, p. pe13
[DOI: 10.1126/scisignal.261pe13]

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Reversible Phosphorylation of Histidine Residues in Proteins from Vertebrates

Susanne Klumpp* and Josef Krieglstein

Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität, D-48149 Münster, Germany.

Abstract: 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 β subunit of heterotrimeric guanosine triphosphate–binding proteins (G proteins), the enzyme adenosine 5'-triphosphate-citrate lyase, and now the Ca2+-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).

* Corresponding author. E-mail, k.secretary{at}uni-muenster.de

Citation: S. Klumpp, J. Krieglstein, Reversible Phosphorylation of Histidine Residues in Proteins from Vertebrates. Sci. Signal. 2, pe13 (2009).

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