Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells

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 wi...

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Bibliographic Details
Published in:FEBS letters 2004-02, Vol.559 (1), p.175-180
Main Authors: Li, Hongbing, Ruano, Marı́a José, Villalobo, Antonio
Format: Article
Language:English
Subjects:
[Ca2+]cyt, cytosolic concentration of free calcium ion
Binding Sites - genetics
Calmodulin
Calmodulin - antagonists & inhibitors
Calmodulin - metabolism
CaM, calmodulin
CaMK-II, calmodulin-dependent protein kinase II
Cell Line, Tumor
Dose-Response Relationship, Drug
EGF, epidermal growth factor
EGFR, EGF receptor
EGTA, [ethylene bis(oxyethylenenitrilo)]-tetraacetic acid
Epidermal growth factor receptor
FBS, fetal bovine serum
Humans
IgG, immunoglobulin G
Kinetics
Living cell
Mutation
Phosphorylation
PMSF, phenylmethylsulfonyl fluoride
Precipitin Tests
Protein Binding
PVDF, polyvinylidene difluoride
Receptor, Epidermal Growth Factor - genetics
Receptor, Epidermal Growth Factor - metabolism
SDS–PAGE, polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate
Sulfonamides - pharmacology
Transfection
W12, N-(4-aminobutyl)-1-naphthalenesulfonamide
W13, N-(4-aminobutyl)-5-chloro-1-naphthalenesulfonamide
W7, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(04)00067-5