Polarity-driven three-dimensional spontaneous rotation of a cell doublet.

First Authors Linjie Lu
Authors Linjie Lu, Tristan Guyomar, Quentin Vagne, Rémi Berthoz, Alejandro Torres-Sánchez, Michèle Lieb, Cécilie Martin-Lemaitre, Kobus van Unen, Alf Honigmann, Olivier Pertz, Guillaume Salbreux, Daniel Riveline
Corresponding Authors
Last Authors Daniel Riveline
Journal Name bioRxiv : the preprint server for biology (bioRxiv)
Article Number doi: https://doi.org/10.1101/2022.12.21.521355
Open Access true
Print Publication Date
Online Publication Date 2022-12-22
Abstract Cell mechanical interactions play a fundamental role in the self-organisation of organisms. How these interactions drive coordinated cell movement in three-dimensions remains unclear. Here we report that cell doublets embedded in a 3D extracellular matrix undergo spontaneous rotations and we investigate the rotation mechanism using live cell imaging, quantitative measurements, mechanical perturbations, and theory. We find that rotation is driven by a polarized distribution of myosin within cell cortices. The mismatched orientation of this polarized distribution breaks the doublet mirror symmetry. In addition, cells adhere at their interface through adherens junctions and with the extracellular matrix through focal contacts near myosin clusters. Using a physical theory describing the doublet as two interacting active surfaces, we find that rotation is driven by myosin-generated gradients of active tension, whose profiles are dictated by interacting cell polarity axes. We show that interface three-dimensional shapes can be understood from the Curie principle: shapes symmetries are related to broken symmetries of myosin distribution in cortices. To test for the rotation mechanism, we suppress myosin clusters using laser ablation and we generate new myosin clusters by optogenetics. Our work clarifies how polarity-oriented active mechanical forces drive collective cell motion in three dimensions.
Cover Image
Affiliated With Honigmann
Selected By
Acknowledged Services
Publication Status Published
Edoc Link
Sfx Link
DOI 10.1101/2022.12.21.521355
PubMed ID
WebOfScience Link
Alternative Full Text URL https://www.biorxiv.org/content/10.1101/2022.12.21.521355v1?ct=ct
Display Publisher Download Only false
Visible On MPI-CBG Website false
PDF Downloadable true
Created By thuem
Added Date 2022-12-28
Last Edited By thuem
Last Edited Date 2022-12-28 11:35:14.211
Library ID 8495
Document ID
Entry Complete true
eDoc Compliant false
Include in Edoc Report false
In Pure false
Ready for eDoc Export false
Author Affiliations Complete false
Project Name
Project URL
Grant ID
Funding Programme
Funding Organisation