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Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 J+Cell+Sci 2016 ; 129 (5): 957-70 Nephropedia Template TP
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KIF17 regulates RhoA-dependent actin remodeling at epithelial cell?cell adhesions #MMPMID26759174
Acharya BR; Espenel C; Libanje F; Raingeaud J; Morgan J; Jaulin F; Kreitzer G
J Cell Sci 2016[Mar]; 129 (5): 957-70 PMID26759174show ga
The kinesin KIF17 localizes at microtubule plus-ends where it contributes to regulation of microtubule stabilization and epithelial polarization. We now show that KIF17 localizes at cell?cell adhesions and that KIF17 depletion inhibits accumulation of actin at the apical pole of cells grown in 3D organotypic cultures and alters the distribution of actin and E-cadherin in cells cultured in 2D on solid supports. Overexpression of full-length KIF17 constructs or truncation mutants containing the N-terminal motor domain resulted in accumulation of newly incorporated GFP?actin into junctional actin foci, cleared E-cadherin from cytoplasmic vesicles and stabilized cell?cell adhesions to challenge with calcium depletion. Expression of these KIF17 constructs also increased cellular levels of active RhoA, whereas active RhoA was diminished in KIF17-depleted cells. Inhibition of RhoA or its effector ROCK, or expression of LIMK1 kinase-dead or activated cofilinS3A inhibited KIF17-induced junctional actin accumulation. Interestingly, KIF17 activity toward actin depends on the motor domain but is independent of microtubule binding. Together, these data show that KIF17 can modify RhoA?GTPase signaling to influence junctional actin and the stability of the apical junctional complex of epithelial cells.