Shared mechanisms regulate spatiotemporal RhoA-dependent actomyosin contractility during adhesion and cell division. (3rd March 2020)

• Record Type: Journal Article
• Authors: Derksen, Patrick W. B.; van de Ven, Robert A. H.
• Is Part Of: Small GTPases. Volume 11:Number 2(2020)
• Page Start: 113
• Page End: 121
• Publication Date: 2020-03-03
• Subjects: cell adhesion -- cytokinesis -- Rho activity -- p120-catenin -- actomyosin contractility; Guanosine triphosphatase -- Periodicals; Guanosine triphosphatase; Periodicals; 572.793
• DOI: 10.1080/21541248.2017.1366966
• Languages: English
• ISSNs: 2154-1256

Abstract

ABSTRACT: 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.