Actin dynamics modulate mechanosensitive immobilization of E-cadherin at adherens junctions

Actin dynamics modulate mechanosensitive immobilization of E-cadherin at adherens junctions
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DOI:
10.1038/ncb2973
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发表时间:
2014-06-01
影响因子:
21.3
通讯作者:
Viasnoff, V.
Viasnoff, V.
中科院分区:
生物学1区
文献类型:
--
作者:
Engl, W.;Arasi, B.;Viasnoff, V.

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机械应力越来越多地被证明是一个有效的调制器的细胞连接形态的发展和稳态过程。因此,细胞间力感测被认为是细胞信号传导和组织完整性的重要调节器。特别是,肌球蛋白收缩性,肌动蛋白动力学和E-钙粘蛋白招聘之间的相互作用在很大程度上仍然有待发现。我们设计了一种悬浮细胞双联体测定,以定量评估肌球蛋白II活性和局部E-钙粘蛋白募集之间的相关性。双联体的单个连接处呈现出典型的形态,E-钙粘蛋白在圆形接触的边缘积聚成不同浓度的簇。这种局部招募成簇来自于通过肌球蛋白II驱动的肌动蛋白周转调节的E-钙粘蛋白的隔离。我们阐明了肌动蛋白动力学的调节如何为细胞接触的机械敏感性反应提供了一种机制。
Mechanical stress is increasingly being shown to be a potent modulator of cell-cell junctional morphologies in developmental and homeostatic processes. Intercellular force sensing is thus expected to be an important regulator of cell signalling and tissue integrity. In particular, the interplay between myosin contractility, actin dynamics and E-cadherin recruitment largely remains to be uncovered. We devised a suspended cell doublet assay to quantitatively assess the correlation between myosin II activity and local E-cadherin recruitment. The single junction of the doublet exhibited a stereotypical morphology, with E-cadherin accumulating into clusters of varied concentrations at the rim of the circular contact. This local recruitment into clusters derived from the sequestration of E-cadherin through a myosin-II-driven modulation of actin turnover. We exemplify how the regulation of actin dynamics provides a mechanism for the mechanosensitive response of cell contacts.