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Published online 19 April 2004. doi:10.1083/jcb.200312118
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 2, 175-180
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 Rab13 regulates PKA signaling during tight junction assembly

Katja Köhler, Daniel Louvard, and Ahmed Zahraoui

Laboratory of Morphogenesis and Cell Signaling, UMR144 Centre National de la Recherche Scientifique, Institut Curie, 75248, Paris, Cedex 05, France

Address correspondence to Ahmed Zahraoui, Laboratory of Morphogenesis and Cell Signaling, Centre National de la Recherche Scientifique, UMR144 Institut Curie, 26 rue d'Ulm, 75248, Paris, Cedex 05, France. Tel.: 33-1-42346370. Fax: 33-1-42346377. email: zahraoui{at}curie.fr

The GTPase Rab13 regulates the assembly of functional epithelial tight junctions (TJs) through a yet unknown mechanism. Here, we show that expression of the GTP-bound form of Rab13 inhibits PKA-dependent phosphorylation and TJ recruitment of the vasodilator-stimulated phosphoprotein, an actin remodelling protein. We demonstrate that Rab13GTP directly binds to PKA and inhibits its activity. Interestingly, activation of PKA abrogates the inhibitory effect of Rab13 on the recruitment of vasodilator-stimulated phosphoprotein, ZO-1, and claudin1 to cell–cell junctions. Rab13 is, therefore, the first GTPase that controls PKA activity and provides an unexpected link between PKA signaling and the dynamics of TJ assembly.

Key Words: Rab GTPase; phosphorylation; VASP; cell–cell junctions; epithelial cells

The online version of this article contains supplemental material.

Abbreviations used in this paper: aPKC{zeta}, atypical PKC{zeta}; P-VASP, phosphorylated VASP; TJ, tight junction; VASP, vasodilator-stimulated phosphoprotein.


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