User:Anat Levit/Sandbox 1: Difference between revisions

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Almost all GPCRs are regulated by phosphorylation and this is a key process in determining the signaling properties of these receptors. Receptors are multiply phosphorylated at sites that can occur throughout the intracellular regions of the receptor. It is well established that GPCR phosphorylation is a complex process involving a range of different protein kinases able to phosphorylate the same receptor at different sites and that this results in differential signaling outcomes, which can be tailored in a tissue specific manner to regulate biological processes.

Almost all GPCRs are regulated by [http://en.wikipedia.org/wiki/Phosphorylation phosphorylation ] and this is a key process in determining the signaling properties of these receptors. Receptors are multiply phosphorylated at sites that can occur throughout the intracellular regions of the receptor. It is well established that GPCR phosphorylation is a complex process involving a range of different protein kinases able to phosphorylate the same receptor at different sites and that this results in differential signaling outcomes, which can be tailored in a tissue specific manner to regulate biological processes.

Sequence analysis of the PKR subtypes revealed that the majority (63%) of putative phosphor-acceptor residues (Ser, Thr and Tyr) are fully conserved between the subtypes, and the rest are either removed in one of the proteins (23%), i.e., the homologues position does not contain a phosphor-acceptor residue, or is changed to another (11%), for example, a switch from Ser to Thr.

We hypnotized that differential signaling of the PKR subtypes may result from phosphorylation of homologues residues by different kinases due to presence of phosphovariants in positions surrounding the phosphor-acceptor residue, and not due to change/elimination of this residue between the subtypes.

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-Almost all GPCRs are regulated by phosphorylation and this is a key process in determining the signaling properties of these receptors. Receptors are multiply phosphorylated at sites that can occur throughout the intracellular regions of the receptor. It is well established that GPCR phosphorylation is a complex process involving a range of different protein kinases able to phosphorylate the same receptor at different sites and that this results in differential signaling outcomes, which can be tailored in a tissue specific manner to regulate biological processes.
+Almost all GPCRs are regulated by [http://en.wikipedia.org/wiki/Phosphorylation phosphorylation ] and this is a key process in determining the signaling properties of these receptors. Receptors are multiply phosphorylated at sites that can occur throughout the intracellular regions of the receptor. It is well established that GPCR phosphorylation is a complex process involving a range of different protein kinases able to phosphorylate the same receptor at different sites and that this results in differential signaling outcomes, which can be tailored in a tissue specific manner to regulate biological processes.
 Sequence analysis of the PKR subtypes revealed that the majority (63%) of putative phosphor-acceptor residues (Ser, Thr and Tyr) are fully conserved between the subtypes, and the rest are either removed in one of the proteins (23%), i.e., the homologues position does not contain a phosphor-acceptor residue, or is changed to another (11%), for example, a switch from Ser to Thr.
 We hypnotized that differential signaling of the PKR subtypes may result from phosphorylation of homologues residues by different kinases due to presence of phosphovariants in positions surrounding the phosphor-acceptor residue, and not due to change/elimination of this residue between the subtypes.