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Molecular and Cellular Biology, March 2006, p. 2247-2261, Vol. 26, No. 6
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.6.2247-2261.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A Spatiotemporally Coordinated Cascade of Protein Kinase C Activation Controls Isoform-Selective Translocation{dagger}

Alejandra Collazos,1,2,{ddagger} Barthélémy Diouf,1,2,{ddagger} Nathalie C. Guérineau,1,3 Corinne Quittau-Prévostel,1,2 Marion Peter,4,§ Fanny Coudane,1,2 Frédéric Hollande,1,2 and Dominique Joubert1,2*

CNRS, UMR5203, INSERM, U661, Université Montpellier I, and Université Montpellier II, Montpellier F-34094, France,1 Cellular and Molecular Oncology Department,2 Endocrinology Department, Institut de Génomique Fonctionnelle, 141 rue de la Cardonille, F-34094 Montpellier Cedex 5, France,3 Randall Division of Cell and Molecular Biophysics, Guy's Campus, King's College London, London SE1 1UL, United Kingdom4

Received 21 November 2005/ Accepted 22 December 2005

In pituitary GH3B6 cells, signaling involving the protein kinase C (PKC) multigene family can self-organize into a spatiotemporally coordinated cascade of isoform activation. Indeed, thyrotropin-releasing hormone (TRH) receptor activation sequentially activated green fluorescent protein (GFP)-tagged or endogenous PKCß1, PKC{alpha}, PKC{varepsilon}, and PKC{delta}, resulting in their accumulation at the entire plasma membrane (PKCß and -{delta}) or selectively at the cell-cell contacts (PKC{alpha} and -{varepsilon}). The duration of activation ranged from 20 s for PKC{alpha} to 20 min for PKC{varepsilon}. PKC{alpha} and -{varepsilon} selective localization was lost in the presence of Gö6976, suggesting that accumulation at cell-cell contacts is dependent on the activity of a conventional PKC. Constitutively active, dominant-negative PKCs and small interfering RNAs showed that PKC{alpha} localization is controlled by PKCß1 activity and is calcium independent, while PKC{varepsilon} localization is dependent on PKC{alpha} activity. PKC{delta} was independent of the cascade linking PKCß1, -{alpha}, and -{varepsilon}. Furthermore, PKC{alpha}, but not PKC{varepsilon}, is involved in the TRH-induced ß-catenin relocation at cell-cell contacts, suggesting that PKC{varepsilon} is not the unique functional effector of the cascade. Thus, TRH receptor activation results in PKCß1 activation, which in turn initiates a calcium-independent but PKCß1 activity-dependent sequential translocation of PKC{alpha} and -{varepsilon}. These results challenge the current understanding of PKC signaling and raise the question of a functional dependence between isoforms.

* Corresponding author. Mailing address: Institut de Génomique Fonctionnelle, 141 rue de la Cardonille, F-34094 Montpellier Cedex 5, France. Phone: (33)-467-142-918. Fax: (33)-467-542-432. E-mail: dominique.joubert{at}igf.cnrs.fr.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} These two authors contributed equally to the paper.

§ Present address: CRBM-CNRS FRE 2593, 1919 route de Mende, 34293 Montpellier Cedex 5, France.

Molecular and Cellular Biology, March 2006, p. 2247-2261, Vol. 26, No. 6
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.6.2247-2261.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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