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Coupling of Rho family GTPases during mesenchymal-to-epithelial-like transitions

Christopher Toret, Pruthvi Shivakumar, Pierre-Francois Lenne, Andre LE BIVIC

Preprint posted on 7 January 2018 https://www.biorxiv.org/content/early/2018/01/07/244343

Elmo-Dock, Arhgap19d and E-Cadherin – A harmonic concert in fruit fly development

Selected by Anh Hoang Le

What are the data?

It has been shown previously that the Elmo2-Dock1 complex regulates the formation of E-Cadherin in MDCK cells [1]. Here, the authors have shown once again this relationship, using a more complex model: dorsal closure during fruit fry development.

Deletion of Elmo, Dock, or both proteins, retains and expands E-Cadherin along the seam line of the dorsal epithelial sheet, but this only happens specifically upon new cell-cell contacts (Figure). This is interesting, as it adds an extra layer of complexity, suggesting a two-way communication between the Elmo-Dock complex and E-Cadherin.

(Toret et al. Figure 1C. Reproduced with permission)

Furthermore, these mutants also have defects in tension modulation, which turns out to be mediated through the Rho1-Myosin II axis. Intriguingly, Myosin II signalling seems to be delayed in the Elmo/Dock mutants, rather than completely abolished. This may hint an unknown compensatory mechanism that is independent of this complex.

Finally, a RhoGAP named Arhgap19d was demonstrated to influence Rac1 activity. A double mutant of both Arhgap19d and Elmo shows a synthetic lethal phenotype, which is thought to be due to the hyperactivity of Rho1.

What I find interesting about this preprint

There are many questions that can be asked. What recruits Elmo-Dock to these new E-Cadherin contact sites? What differentiates these new contact sites from the older ones? How are Elmo-Dock and Arhgap19d coordinated in the first place? Is the regulation of Rac1 by Arhgap19d a result of a direct interaction, or merely due to its effect on Rho1?

In the context of cancer metastasis, this study has shed some new light on the process of mesenchymal-to-epithelial transition (MET). Disseminated cancer cells need to undergo this process in order to establish new colonies. It is known that during MET, a cancer cell can switch on its epithelial status, re-expressing the previously lost E-Cadherin. What is the signalling outcome when cancer cells engage in a similar E-Cadherin interaction? Moreover, what are the consequences of a heterotypic interaction between E-Cadherin and another type of Cadherins? Based on this study, this can have consequences on at least the localisation and functions of RhoGTPases and their effectors. By understanding these signalling events, we will be better at understanding how disease processes happen and how to prevent them.

[1] Toret, C. (2014) An Elmo–Dock complex locally controls Rho GTPases and actin remodeling during cadherin-mediated adhesion. JCB, 207 (5): 577 DOI: 10.1083/jcb.201406135

Thanks to Nikki Paul (CRUK Beatson) for the comments on my highlight.

Note: the preprint has recently been published in Development (see final version here).

 

 

 

Posted on: 13 February 2018 , updated on: 19 February 2018

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