Journal article

A 20-Amino Acid Module of Protein Kinase C epsilon Involved in Translocation and Selective Targeting at Cell-Cell Contacts

Barthelemy Diouf, Alejandra Collazos, Gilles Labesse, Francoise Macari, Armelle Choquet, Philippe Clair, Cecile Gauthier-Rouviere, Nathalie C Guerineau, Philippe Jay, Frederic Hollande, Dominique Joubert

Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2009


In the pituitary gland, activated protein kinase C (PKC) isoforms accumulate either selectively at the cell-cell contact (alpha and epsilon) or at the entire plasma membrane (beta1 and delta). The molecular mechanisms underlying these various subcellular locations are not known. Here, we demonstrate the existence within PKCepsilon of a cell-cell contact targeting sequence (3CTS) that, upon stimulation, is capable of targeting PKCdelta, chimerin-alpha1, and the PKCepsilon C1 domain to the cell-cell contact. We show that this selective targeting of PKCepsilon is lost upon overexpression of 3CTS fused to a (R-Ahx-R)(4) (where Ahx is 6-aminohexanoic acid) vectorization peptide, reflecting a domi..

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University of Melbourne Researchers