期刊
JOURNAL OF CELL BIOLOGY
卷 165, 期 2, 页码 175-180出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200312118
关键词
Rab GTPase; phosphorylation; VASP; cell-cell junctions; epithelial cells
类别
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.
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