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

Small GTPases. 2020 Mar;11(2):113-121. doi: 10.1080/21541248.2017.1366966. Epub 2017 Dec 31.


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.

Keywords: Rho activity; actomyosin contractility; cell adhesion; cytokinesis; p120-catenin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actomyosin / metabolism*
  • Animals
  • Cell Adhesion*
  • Cell Division*
  • Cytokinesis
  • Humans
  • Spatio-Temporal Analysis
  • rhoA GTP-Binding Protein / metabolism*


  • Actomyosin
  • rhoA GTP-Binding Protein

Grant support

Netherlands Organization for Scientific Research (NWO/ZonMW-VIDI 0616.096.318); Dutch Cancer Society (KWF-UU-2011-5230).