Crumbs is an essential regulator of cytoskeletal dynamics and cell-cell adhesion during dorsal closure in Drosophila

Flores-Benítez, David; Knust, Elisabeth

doi:10.7554/elife.07398

Cited by 45 publications

(59 citation statements)

References 179 publications

(255 reference statements)

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“…Mbs dephosphorylates Moesin in the AS and not in the epidermis, suggesting that this is a tissuespecific effect. Interestingly, it has recently been reported that an AS-specific function of Crumbs involving its FERM binding domain also affects actomyosin contractility and adhesion in this tissue (Flores-Benitez and Knust, 2015). In that work, a phosphomimetic form of Moesin was able to rescue the defects caused by this particular Crumbs mutant.…”

Section: Mbs As Coordinator Of Cytoskeletal Activity and Adhesionmentioning

confidence: 50%

Integration of actomyosin contractility with cell-cell adhesion during dorsal closure

Duque

Gorfinkiel

2016

Development

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In this work, we combine genetic perturbation, time-lapse imaging and quantitative image analysis to investigate how pulsatile actomyosin contractility drives cell oscillations, apical cell contraction and tissue closure during morphogenesis of the amnioserosa, the main force-generating tissue during the dorsal closure in Drosophila. We show that Myosin activity determines the oscillatory and contractile behaviour of amnioserosa cells. Reducing Myosin activity prevents cell shape oscillations and reduces cell contractility. By contrast, increasing Myosin activity increases the amplitude of cell shape oscillations and the time cells spend in the contracted phase relative to the expanded phase during an oscillatory cycle, promoting cell contractility and tissue closure. Furthermore, we show that in AS cells, Rok controls Myosin foci formation and Mbs regulates not only Myosin phosphorylation but also adhesion dynamics through control of Moesin phosphorylation, showing that Mbs coordinates actomyosin contractility with cell-cell adhesion during amnioserosa morphogenesis.

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Section: Mbs As Coordinator Of Cytoskeletal Activity and Adhesionmentioning

confidence: 50%

Integration of actomyosin contractility with cell-cell adhesion during dorsal closure

Duque

Gorfinkiel

2016

Development

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“…Fourth, we still do not understand what directs the location of an actomyosin pulse. Fifth, we advocate searches for proteins outside of the core actomyosin machinery, for example aPKC (David et al, 2013) and Crumbs (Flores-Benitez et al, 2015), that impinge on actomyosin dynamics. Finally, we are excited about using the newest generation of in vivo biomechanical sensors, like lipid droplets embedded in epithelia (Campàs et al, 2014) or single-walled carbon nanotubules (Tan et al, 2016) that can provide direct measurements of the material properties of cells and tissues experiencing dynamic actomyosin contractility.…”

Section: Discussionmentioning

confidence: 99%

Actomyosin Pulsing in Tissue Integrity Maintenance during Morphogenesis

Coravos

Mason

Martin

2017

Trends in Cell Biology

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Summary The actomyosin cytoskeleton is responsible for many changes in cell and tissue shape. For a long time, the actomyosin cytoskeleton has been known to exhibit dynamic contractile behavior. Recently, discrete actomyosin assembly/disassembly cycles have also been observed in cells. These so-called actomyosin pulses have been observed in a variety of contexts, including cell polarization and division, and in epithelia, where they occur during tissue contraction, folding, and extension. In epithelia, evidence suggests that actomyosin pulsing, and more generally, actomyosin turnover, is required to maintain tissue integrity during contractile processes. This review explores possible functions for pulsing in the many instances during which pulsing has been observed, and also highlights proposed molecular mechanisms that drive pulsing.

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“…Our data support the hypothesis that the Sdt-Crb complex is specifically required in polarizing cells undergoing fast AJ turnover, whereas in polarized cells biosynthetically stable AJs make Sdt-Cbr dispensable. Interestingly, DE-CadASSA or DE-CadS4A-αCat did not rescue Baz localization in amnioserosa cells in crb KO or sdt KO mutant embryos (data not shown), suggesting that the Sdt-Crb complex acts through mechanisms independent of AJ stability to maintain polarity in these actively constricting cells (David et al, 2010;Flores-Benitez and Knust, 2015;Harden et al, 2002).…”

Section: Conserved Serine Residues Regulate the Biosynthetic Turnovermentioning

confidence: 99%

Phosphorylation potential of Drosophila E-Cadherin intracellular domain is essential for development and adherens junction biosynthetic dynamics regulation

Chen

Huang

et al. 2017

Development

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Phosphorylation of a highly conserved serine cluster in the intracellular domain of E-Cadherin is essential for binding to β-Catenin in vitro. In cultured cells, phosphorylation of specific serine residues within the cluster is also required for regulation of adherens junction (AJ) stability and dynamics. However, much less is known about how such phosphorylation of E-Cadherin regulates AJ formation and dynamics in vivo. In this report, we generated an extensive array of Drosophila E-Cadherin (DE-Cad) endogenous knock-in alleles that carry mutations targeting this highly conserved serine cluster. Analyses of these mutations suggest that the overall phosphorylation potential, rather than the potential site-specific phosphorylation, of the serine cluster enhances the recruitment of β-Catenin by DE-Cad in vivo. Moreover, phosphorylation potential of the serine cluster only moderately increases the level of β-Catenin in AJs and is in fact dispensable for AJ formation in vivo. Nonetheless, phosphorylation-dependent recruitment of β-Catenin is essential for development, probably by enhancing the interactions between DECad and α-Catenin. In addition, several phospho-mutations dramatically reduced the biosynthetic turnover rate of DE-Cad during apical-basal polarization, and such biosynthetically stable DE-Cad mutants specifically rescued the polarity defects in embryonic epithelia lacking the polarity proteins Stardust and Crumbs.

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Crumbs is an essential regulator of cytoskeletal dynamics and cell-cell adhesion during dorsal closure in Drosophila

Cited by 45 publications

References 179 publications

Integration of actomyosin contractility with cell-cell adhesion during dorsal closure

Integration of actomyosin contractility with cell-cell adhesion during dorsal closure

Actomyosin Pulsing in Tissue Integrity Maintenance during Morphogenesis

Phosphorylation potential of Drosophila E-Cadherin intracellular domain is essential for development and adherens junction biosynthetic dynamics regulation

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