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PMID:14960328
| Citation |
Li, H, Ruano, MJ and Villalobo, A (2004) Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett. 559:175-80 |
|---|---|
| Abstract |
We have previously shown that exogenous calmodulin (CaM) binds to the epidermal growth factor receptor (EGFR) at its cytosolic juxtamembrane region inhibiting its tyrosine kinase activity. We demonstrate in this report that endogenous CaM binds to EGFR in intact cells as CaM co-immunoprecipitates with EGF-activated and non-activated receptors. We also show in living cells that cell-permeable CaM inhibitors prevent the full transphosphorylation of wild type EGFR but not the transphosphorylation of an insertional EGFR mutant in which the CaM-binding domain was divided into two parts. Overall these results suggest that CaM interacts with EGFR in vivo. |
| Links |
PubMed Online version:10.1016/S0014-5793(04)00067-5 |
| Keywords |
Binding Sites/genetics; Calmodulin/antagonists & inhibitors; Calmodulin/metabolism; Cell Line, Tumor; Dose-Response Relationship, Drug; Humans; Kinetics; Mutation; Phosphorylation; Precipitin Tests; Protein Binding; Receptor, Epidermal Growth Factor/genetics; Receptor, Epidermal Growth Factor/metabolism; Sulfonamides/pharmacology; Transfection |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0005515: protein binding |
IPI: Inferred from Physical Interaction: UniProtKB:P62204 |
F |
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| GO:0005515: protein binding |
IPI: Inferred from Physical Interaction: UniProtKB:P62158 |
F |
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See also
References
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