Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Catimel, B. et al.

In situ phosphorylation of immobilized receptors on biosensor surfaces: Application to E-cadherin/beta-catenin interactions.

Phosphorylation is a key posttranslational modification for modulating biological interactions. Biosensor technology is ideally suited for examining in real time the role of phosphorylation on protein-protein interactions in signaling pathways. We have developed processes for on-chip phosphorylation of immobilized receptors on biosensor surfaces. These processes have been used to analyze E-cadherin/beta-catenin interactions. Phosphorylation of the intracellular domain (ICD) of E-cadherin modulates its affinity to beta-catenin and consequently the strength of cell-cell adhesion. We have phosphorylated immobilized E-cadherin ICD in situ using casein kinase 1 (CK1), casein kinase 2 (CK2), and src. On-chip phosphorylation of E-cadherin was confirmed using anti-phosphoserine and anti-phosphotyrosine antibodies. The binding of beta-catenin to E-cadherin was analyzed quantitatively. CK1 phosphorylation of E-cadherin increased the binding affinity to beta-catenin from approximately 230 to 4nM. A similar increase in affinity, from 260 to 4nM, was obtained with CK2 phosphorylation of E-cadherin. However, phosphorylation by src kinase decreased the affinity constant from approximately 260nM to 4muM. Interestingly, phosphorylation of E-cadherin by CK1 or CK2 prevented the inhibition of beta-catenin binding by src phosphorylation.[1]

References

In situ phosphorylation of immobilized receptors on biosensor surfaces: Application to E-cadherin/beta-catenin interactions. Catimel, B., Layton, M., Church, N., Ross, J., Condron, M., Faux, M., Simpson, R.J., Burgess, A.W., Nice, E.C. Anal. Biochem. (2006) [Pubmed]

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