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Small GTPases. 2017 Dec 31:1-9. doi: 10.1080/21541248.2017.1366966. [Epub ahead of print]

Shared mechanisms regulate spatiotemporal RhoA-dependent actomyosin contractility during adhesion and cell division.

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a Department of Pathology , University Medical Center Utrecht , Heidelberglaan CX Utrecht , the Netherlands.
b Department of Cell Biology , Harvard Medical School , 240 Longwood Avenue Boston , MA , USA.


Local modulation of the actin cytoskeleton is essential for the initiation and maintenance of strong homotypic adhesive interfaces between neighboring cells. The epithelial adherens junction (AJ) fulfils a central role in this process by mediating E-cadherin interactions and functioning as a signaling scaffold to control the activity of the small GTPase RhoA and subsequent actomyosin contractility. Interestingly, a number of regulatory proteins that modulate RhoA activity at the AJ also control RhoA during cytokinesis, an actomyosin-dependent process that divides the cytoplasm to generate two daughter cells at the final stages of mitosis. Recent insights have revealed that the central player in AJ stability, p120-catenin (p120), interacts with and modulates essential regulators of actomyosin contraction during cytokinesis. In cancer, loss of this modulation is a common event during tumor progression that can induce chromosomal instability and tumor progression. In this review, we will highlight the functional differences and similarities of the different RhoA-associated factors that have been linked to both the regulation of cell-cell adhesion and cytokinesis.


Rho activity; actomyosin contractility; cell adhesion; cytokinesis; p120-catenin

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