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Title: Protein KinaseCdelta-Calmodulin Crosstalk Regulates Epidermal Growth Factor Receptor Exit from Early Endosomes
Author: Lladó, Anna
Tebar Ramon, Francesc
Calvo Ademuz, Maria
Moretó Elias, Jemina
Sorkin, Alexander
Enrich Bastús, Carles
Keywords: Calmodulina
Factor de creixement epidèrmic
Proteïnes quinases
Epidermal growth factor
Protein kinases
Issue Date: 23-Aug-2004
Publisher: American Society for Cell Biology
Abstract: We have recently shown that calmodulin antagonist W13 interferes with the trafficking of the epidermal growth factor receptor (EGFR) and regulates the mitogen-activated protein kinase (MAPK) signaling pathway. In the present study, we demonstrate that in cells in which calmodulin is inhibited, protein kinase C (PKC) inhibitors rapidly restore EGFR and transferrin trafficking through the recycling compartment, although onward transport to the degradative pathway remains arrested. Analysis of PKC isoforms reveals that inhibition of PKCδ with rottlerin or its down-modulation by using small interfering RNA is specifically responsible for the release of the W13 blockage of EGFR trafficking from early endosomes. The use of the inhibitor Go 6976, specific for conventional PKCs (α, β, and γ), or expression of dominant-negative forms of PKCλ, ζ, or e did not restore the effects of W13. Furthermore, in cells treated with W13 and rottlerin, we observed a recovery of brefeldin A tubulation, as well as transport of dextran-fluorescein isothiocyanate toward the late endocytic compartment. These results demonstrate a specific interplay between calmodulin and PKCδ in the regulation of the morphology of and trafficking from the early endocytic compartment.
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It is part of: Molecular Biology of the Cell, 2004, vol. 15, núm. 11, p. 4877-4891
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ISSN: 1059-1524
Appears in Collections:Articles publicats en revistes (Biomedicina)

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