KIF17 regulates RhoA-dependent actin remodeling at epithelial cell-cell adhesions

Acharya, Bipul R., Espenel, Cedric, Libanje, Fotine, Raingeaud, Joel, Morgan, Jessica, Jaulin, Fanny and Kreitzer, Geri (2016) KIF17 regulates RhoA-dependent actin remodeling at epithelial cell-cell adhesions. Journal of Cell Science, 129 5: 957-970. doi:10.1242/jcs.173674

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Author Acharya, Bipul R.
Espenel, Cedric
Libanje, Fotine
Raingeaud, Joel
Morgan, Jessica
Jaulin, Fanny
Kreitzer, Geri
Title KIF17 regulates RhoA-dependent actin remodeling at epithelial cell-cell adhesions
Journal name Journal of Cell Science   Check publisher's open access policy
ISSN 1477-9137
Publication date 2016-03-01
Year available 2016
Sub-type Article (original research)
DOI 10.1242/jcs.173674
Open Access Status File (Publisher version)
Volume 129
Issue 5
Start page 957
End page 970
Total pages 14
Place of publication Cambridge, United Kingdom
Publisher Company of Biologists
Language eng
Formatted abstract
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.
Keyword Rho-GTPases
Cell-cell adhesion
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID R01GM087575
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
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