Actin Rings of Power

Schwayer, Cornelia; Sikora, Mateusz; Slováková, Jana; Kardos, Roland; Heisenberg, Carl‐Philipp

doi:10.1016/j.devcel.2016.05.024

Cited by 87 publications

(82 citation statements)

References 186 publications

(212 reference statements)

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“…This thereby allows both actin structures to co-exist in condition of low RhoA activity. Actomyosin rings are critical cytoskeletal structures contributing to essential processes, such as cytokinesis and wound healing, in epithelia944454647. Actomyosin ring is also critical to adjust the size of tunnels between endothelial cells when neutrophils undergo endothelial diapedesis8.…”

Section: Discussionmentioning

confidence: 99%

Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation

et al. 2017

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Transendothelial cell macroaperture (TEM) tunnels control endothelium barrier function and are triggered by several toxins from pathogenic bacteria that provoke vascular leakage. Cellular dewetting theory predicted that a line tension of uncharacterized origin works at TEM boundaries to limit their widening. Here, by conducting high-resolution microscopy approaches we unveil the presence of an actomyosin cable encircling TEMs. We develop a theoretical cellular dewetting framework to interpret TEM physical parameters that are quantitatively determined by laser ablation experiments. This establishes the critical role of ezrin and non-muscle myosin II (NMII) in the progressive implementation of line tension. Mechanistically, fluorescence-recovery-after-photobleaching experiments point for the upstream role of ezrin in stabilizing actin filaments at the edges of TEMs, thereby favouring their crosslinking by NMIIa. Collectively, our findings ascribe to ezrin and NMIIa a critical function of enhancing line tension at the cell boundary surrounding the TEMs by promoting the formation of an actomyosin ring.

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Section: Discussionmentioning

confidence: 99%

Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation

et al. 2017

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“…Apical constriction is driven by cortical tension-generating actomyosin contractions that are transmitted to neighboring cells via apically localized cadherins (reviewed in [Heisenberg and Bellaïche, 2013; Martin et al, 2009; Pilot and Lecuit, 2005; Schwayer et al, 2016]). We demonstrate that Fgf-dependent Notch signaling cell-autonomously, and downstream of Fgf signaling upregulates adherens and tight junction molecules.…”

Section: Introductionmentioning

confidence: 99%

Proliferation-independent regulation of organ size by Fgf/Notch signaling

Kozlovskaja-Gumbrienė

Ren

Richard

et al. 2017

eLife

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Organ morphogenesis depends on the precise orchestration of cell migration, cell shape changes and cell adhesion. We demonstrate that Notch signaling is an integral part of the Wnt and Fgf signaling feedback loop coordinating cell migration and the self-organization of rosette-shaped sensory organs in the zebrafish lateral line system. We show that Notch signaling acts downstream of Fgf signaling to not only inhibit hair cell differentiation but also to induce and maintain stable epithelial rosettes. Ectopic Notch expression causes a significant increase in organ size independently of proliferation and the Hippo pathway. Transplantation and RNASeq analyses revealed that Notch signaling induces apical junctional complex genes that regulate cell adhesion and apical constriction. Our analysis also demonstrates that in the absence of patterning cues normally provided by a Wnt/Fgf signaling system, rosettes still self-organize in the presence of Notch signaling.DOI: http://dx.doi.org/10.7554/eLife.21049.001

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“…Finally, we found that p120-catenin levels altered the tension of the plasma membrane. Altogether, this shows that p120-catenin is a central hub which co-ordinates cell adhesion, endocytosis, and actin dynamics with tissue tension.requires Rho-kinase for recruitment to AJs [76][77][78].…”

mentioning

confidence: 85%

E-cadherin endocytosis is modulated by p120-catenin through the opposing actions of RhoA and Arf1

Greig

Bulgakova

2018

Preprint

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The regulation of E-cadherin at the plasma membrane by endocytosis is of vital importance for developmental and disease. p120-catenin, which binds to the E-cadherin C-terminus, can both promote and inhibit E-cadherin endocytosis. However, little is known about what determines the directionality of p120-catenin activity, and the molecules downstream. Here, we have discovered that p120-catenin fine-tunes the clathrin-mediated endocytosis of Ecadherin in Drosophila embryonic epidermal cells. It simultaneously activated two actinremodelling pathways with opposing effects: RhoA, which stabilized E-cadherin at the membrane, and Arf1, which promoted internalization. Epistasis experiments revealed that RhoA additionally inhibited Arf1. E-cadherin was efficiently endocytosed only in the presence of intermediate p120-catenin amounts with too little and too much p120-catenin inhibiting E-cadherin endocytosis. Finally, we found that p120-catenin levels altered the tension of the plasma membrane. Altogether, this shows that p120-catenin is a central hub which co-ordinates cell adhesion, endocytosis, and actin dynamics with tissue tension.requires Rho-kinase for recruitment to AJs [76][77][78].

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Actin Rings of Power

Cited by 87 publications

References 186 publications

Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation

Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation

Proliferation-independent regulation of organ size by Fgf/Notch signaling

E-cadherin endocytosis is modulated by p120-catenin through the opposing actions of RhoA and Arf1

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