Cytocortex-dependent dynamics of Drosophila Crumbs controls junctional stability and tension during germ band retraction.

First Authors Anna Bajur
Authors Anna Bajur, K Venkatesan Iyer, Elisabeth Knust
Corresponding Authors Elisabeth Knust
Last Authors Elisabeth Knust
Journal Name Journal of cell science (J Cell Sci)
Volume 132
Issue 15
Article Number jcs228338
Open Access false
Print Publication Date 2019-08-07
Online Publication Date
Abstract During morphogenesis, epithelia undergo dynamic rearrangements, which requires continuous remodelling of junctions and cell shape, but at the same time mechanisms preserving cell polarity and tissue integrity. Apico-basal polarity is key for the localisation of the machinery that enables cell shape changes. The evolutionarily conserved Drosophila Crumbs protein is critical for maintaining apico-basal polarity and epithelial integrity. How Crumbs is maintained in a dynamically developing embryo remains largely unknown. Here, we applied quantitative fluorescence techniques to show that, during germ band retraction, Crumbs dynamics correlates with the morphogenetic activity of the epithelium. Genetic and pharmacological perturbations revealed that the mobile pool of Crumbs is fine-tuned by the actomyosin cortex in a stage-dependent manner. Stabilisation of Crumbs at the plasma membrane depends on a proper link to the actomyosin cortex via an intact FERM-domain-binding site in its intracellular domain, loss of which leads to increased junctional tension and higher DE-cadherin (also known as Shotgun) turnover, resulting in impaired junctional rearrangements. These data define Crumbs as a mediator between polarity and junctional regulation to orchestrate epithelial remodelling in response to changes in actomyosin activity.This article has an associated First Person interview with the first author of the paper.
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Affiliated With Eaton, Knust, Postdoc first author, Postdocs, Postdoc first female
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Acknowledged Services Scientific Computing Facility, Light Microscopy Facility
Publication Status Published
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DOI 10.1242/jcs.228338
PubMed ID 31300472
WebOfScience Link WOS:000481589200011
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Created By thuem
Added Date 2019-08-07
Last Edited By herbst
Last Edited Date 2021-04-29 16:45:28.181
Library ID 7462
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