Actomyosin tension is required for correct recruitment of adherens junction components and zonula occludens formation

Miyake, Yuka; Inoue, N.; Nishimura, Koji; Kinoshita, N.; Hosoya, Hiroshi; Yonemura, Shigenobu

doi:10.1016/j.yexcr.2006.01.031

Cited by 155 publications

(167 citation statements)

References 55 publications

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“…We demonstrated that attachment of monocytes to endothelial cells or overexpression of CA-H-Ras in endothelial cells recruits Src to the VE-cad complex (14,17). Furthermore, the earlier findings demonstrated that actin polymerization, Rho A activity, and activity of myosin are required for recruitment and accumulation of junctional complex components (36,37).…”

Section: Discussionmentioning

confidence: 52%

Integrin α2β1 Mediates Tyrosine Phosphorylation of Vascular Endothelial Cadherin Induced by Invasive Breast Cancer Cells

Haidari

Zhang

Caivano

et al. 2012

Journal of Biological Chemistry

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Background:The disruption of endothelial barrier function by tumor cells was studied. Results: The attachment of tumor cells to endothelial cells leads to the disorganization of endothelial adherens junction. Conclusion: Interaction of tumor cells with endothelial cells alters endothelial signaling and facilitates cancer cell diapedesis. Significance: This study introduces new therapeutic targets for treating metastatic breast cancer.

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Section: Discussionmentioning

confidence: 52%

Integrin α2β1 Mediates Tyrosine Phosphorylation of Vascular Endothelial Cadherin Induced by Invasive Breast Cancer Cells

Haidari

Zhang

Caivano

et al. 2012

Journal of Biological Chemistry

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“…NM-IIdependent recruitment of vinculin to AJs revealed a mechanosensing role for E-cadherin (le Duc et al 2010). Yonemura and colleagues showed an NM-II-dependent mechanism for stabilization of AJs that involves a forcedependent interaction between vinculin and a-catenin (Miyake et al 2006;Yonemura et al 2010). Further, direct application of an exogenous tugging force was sufficient, in addition to myosin activity, to trigger AJ formation and stabilization .…”

Section: Ajs As Mechanosensorsmentioning

confidence: 99%

Phosphoinositides in Cell Architecture

Shewan

Eastburn²,

Mostov

2011

Cold Spring Harbor Perspectives in Biology

173

159

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Inositol phospholipids have been implicated in almost all aspects of cellular physiology including spatiotemporal regulation of cellular signaling, acquisition of cellular polarity, specification of membrane identity, cytoskeletal dynamics, and regulation of cellular adhesion, motility, and cytokinesis. In this review, we examine the critical role phosphoinositides play in these processes to execute the establishment and maintenance of cellular architecture. Epithelial tissues perform essential barrier and transport functions in almost all major organs. Key to their development and function is the establishment of epithelial cell polarity. We place a special emphasis on highlighting recent studies demonstrating phosphoinositide regulation of epithelial cell polarity and how individual cells use phosphoinositides to further organize into epithelial tissues.P hosphoinositides (PIs) are essential components of cellular membranes in eukaryotes. Though these specialized lipids comprise less than 1% of the cellular lipid cohort, they play key roles in many fundamental biological processes (Di Paolo and De Camilli 2006;Saarikangas et al. 2010). PIs possess such far ranging roles by serving as specialized membrane docking sites for effectors of numerous cellular signal transduction cascades. PIs also serve as precursors of lipid second messengers. They are concentrated on the cytosolic face of cellular membranes (Fig. 1A) and rapidly diffuse within the plane of the membrane. Reversible phosphorylation of the myo-inositol head group of phosphatidylinositol (PtdIns) at positions 3, 4, and 5 (Fig. 1B) gives rise to the seven PI isoforms identified in eukaryotic cells. PtdIns(4)P and PtdIns(4,5)P 2 are constitutively present in membranes and comprise the largest pool of cellular PIs, whereas PtdIns(3,4,5)P 3 is essentially undetectable in most types of unstimulated cells (Lemmon and Ferguson 2000;Saarikangas et al. 2010).The spatiotemporally regulated production and turnover of phosphoinositides is crucial for localized PI signaling and function. Numerous phosphatidylinositol kinases and phosphatases are involved in regulating the metabolism of the various PI isoforms (Fig. 1)

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“…At PAs actin filaments associate with the plasma membrane in a perpendicular manner (6, 11, 15, 21 -24), enabling direct transmission of forces through AJs to adjacent cells ( Figure 1A, D). When forces are reduced by inhibiting myosin II activity, PAs cannot be maintained and are converted into ZAs (25,26). Normally PAs convert into ZAs during sheet formation of highly polarized epithelial cells (11,15,23).…”

Section: Ultrastructure Of Actin Filament/aj As-sociationmentioning

confidence: 99%

“…It has actin binding region in its C-terminus, which is exposed when vinculin is activated (42). As vinculin recruitment to focal adhesions is forcedependent (43), vinculin recruitment to AJs through its binding to α-catenin is also force-dependent (26,44,45). Although the cadherin -catenin complex distribution along the lateral membranes is not affected in epithelial sheets when myosin II activity is inhibited, vinculin disappears from ZAs.…”

Section: Aj Components Responsible For Actin As-sociationmentioning

confidence: 99%

Actin filament association at adherens junctions

Yonemura

2017

J. Med. Invest.

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: The adherens junction (AJ) is a cadherin-based and actin filament associated cell-to-cell junction. AJs can contribute to tissue morphogenesis and homeostasis and their association with actin filaments is crucial for the functions. There are three types of AJs in terms of the mode of actin filament/AJ association. Among many actin-binding proteins associated with AJs, α-catenin is one of the most important actin filament/AJ linkers that functions in all types of AJs. Although α-catenin in cadherin-catenin complex appears to bind to actin filaments within cells, it fails to bind to actin filaments in vitro mysteriously. Recent report revealed that α-catenin in the complex can bind to actin filaments in vitro when forces are applied to the filament. In addition to force-sensitive vinculin binding, α-catenin has another force-sensitive property of actin filament-binding. Elucidation of its significance and the molecular mechanism is indispensable for understanding AJ formation and maintenance during tissue morphogenesis, function and repair.

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Actomyosin tension is required for correct recruitment of adherens junction components and zonula occludens formation

Cited by 155 publications

References 55 publications

Integrin α2β1 Mediates Tyrosine Phosphorylation of Vascular Endothelial Cadherin Induced by Invasive Breast Cancer Cells

Integrin α2β1 Mediates Tyrosine Phosphorylation of Vascular Endothelial Cadherin Induced by Invasive Breast Cancer Cells

Phosphoinositides in Cell Architecture

Actin filament association at adherens junctions

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