Protein phosphorylation is a common modification employed by cells to alter protein function. We hypothesize that phosphorylation by activated protein kinase C performs a negative feedback role in phospholipid-dependent signaling to alter the function of some or all of the proteins in the signaling pathway. Using purified signaling proteins and protein kinases we have been studying the phosphorylation of PLC- b enzymes in detail at a molecular level.
Signal desensitization can be a mechanism to avoid cell over-stimulation.
Conversely, de-regulated signaling pathways are responsible for some kinds of malignant cell transformation. Clinically, targets for lengthening the duration of action of therapeutics may be designed based on a better understanding of desensitization of signal transduction pathways. IRL Press at Oxford University Press . Structure, pharmacological selectivity, and second messenger signaling properties of G protein-coupled P2 purinergic receptors. John Wiley and Sons .