Cell Responses Initiated by Ecto-Kinases

  • Jeffrey S. Fedan
Part of the The Receptors book series (REC)


The effects of extracellular adenosine triphosphate (ATP) on cells clearly involve binding interactions with P2 receptors, which initiate transduction and responses mediated by intracellular messengers. It is tacitly assumed that, like non-nucleotide agonists, the binding of ATP and its synthetic congeners at the receptors involves a reversible association-dissociation phenomenon in which this high energy phosphate-containing nucleotide is not changed chemically as a consequence. Much evidence indicates that, in addition to the extracellular receptors for ATP, many types of cells possess on their outer membrane surface one or more kinase enzymes, referred to as “ecto-kinases” (“EK”) because of their location, that utilize the γ-phosphate of ATP to phos-phorylate proteins. The phosphorylated proteins may reside in or on the cell membrane, in which case they are referred to as “endogenous” substrates. EK may also phosphorylate proteins in the extracellular milieu; these substrates are referred to as “exogenous” substrates. The relationship of these phosphorylation events to cell processes is not apparent in most cases. There are a few examples in which the relationship between phosphorylation and function seem well correlated, but usually the biochemical evidence for phosphorylation precedes and is better established than functional significance.


Atrial Natriuretic Peptide Endogenous Substrate Exogenous Substrate Phosphoryl Transfer Affinity Label 
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© Springer Science+Business Media New York 1998

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  • Jeffrey S. Fedan

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