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Vol. 15, Issue 11, 4877-4891, November 2004

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Protein KinaseC-Calmodulin Crosstalk Regulates Epidermal Growth Factor Receptor Exit from Early Endosomes

Anna Lladó ^* , Francesc Tebar ^* , Maria Calvo ^*, Jemina Moretó ^*, Alexander Sorkin , and Carlos Enrich ^* 

^* Departament de Biologia Cellular, Facultat de Medicina, Universitat de Barcelona, 08036 Barcelona, Spain; Department of Pharmacology, Health Science Center, University of Colorado, Denver, CO 80262

Submitted February 13, 2004; Revised August 20, 2004; Accepted August 23, 2004
Monitoring Editor: Keith Mostov

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 PKC 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 Gö 6976, specific for conventional PKCs (, , and ), or expression of dominant-negative forms of PKC, , or 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 PKC in the regulation of the morphology of and trafficking from the early endocytic compartment.

These authors contributed equally to this work.

Corresponding author. E-mail address: enrich{at}ub.edu.

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