Actin filament association at adherens junctions

Yonemura, Shigenobu

doi:10.2152/jmi.64.14

Cited by 21 publications

(19 citation statements)

References 64 publications

(31 reference statements)

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“…Indeed, mDia1 regulates junctional tension by reorganizing actin into actomyosin bundles at the AJ in Caco-2 colon epithelial cells [64]. This is significant given that α-catenin binding to both F-actin and the actin-binding protein vinculin are force-dependent due to conformational changes in α-catenin that occur with force application [6, 65]. As mDia2 is important for junctional stability and resistance to shear force in EOC cells (Figure 1), it is reasonable to surmise that mDia2 stabilizes junctions by providing contractile force at the AJ.…”

Section: Discussionmentioning

confidence: 99%

mDia2 formin selectively interacts with catenins and not E-cadherin to regulate Adherens Junction formation

Zhang

Pettee

Becker

et al. 2019

Preprint

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24 Background: Epithelial ovarian cancer (EOC) cells disseminate within the 25 peritoneal cavity, in part, via the peritoneal fluid as single cells, clusters, or 26 spheroids. Initial single cell egress from a tumor can involve disruption of cell-cell 27 adhesions as cells are shed from the primary tumor into the peritoneum. In 28 epithelial cells, Adherens Junctions (AJs) are characterized by homotypic linkage 29 of E-cadherins on the plasma membranes of adjacent cells. AJs are anchored to 30 the intracellular actin cytoskeletal network through a complex involving E-31 cadherin, p120 catenin, b-catenin, and aE-catenin. However, the specific players 32 involved in the interaction between the junctional E-cadherin complex and the 33 underlying F-actin network remains unclear. Recent evidence indicates that 34 mammalian Diaphanous-related (mDia) formins plays a key role in epithelial cell 35 AJ formation and maintenance through generation of linear actin filaments. 36 Binding of aE-catenin to linear F-actin inhibits association of the branched-actin 37 nucleator Arp2/3, while favoring linear F-actin bundling. We previously 38 demonstrated that loss of mDia2 was associated with invasive single cell egress 39 from EOC spheroids through disruption of junctional F-actin. 40 41 Results: In the current study, we now show that mDia2 has a role at adherens 42 junctions (AJs) in EOC OVCA429 cells and human embryonic kidney (HEK) 293 43 cells through its association with aE-catenin and b-catenin. mDia2 depletion in 44 EOC cells leads to reduction in actin polymerization and disruption of cell-cell 45 junctions with decreased interaction between b-catenin and E-cadherin. 46 3 47 Conclusions: Our results support a necessary role for mDia2 in AJ stability in 48 EOC cell monolayers and indicate a critical role for mDia formins in regulating 49 EOC AJs during invasive transitions. 50 51

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Section: Discussionmentioning

confidence: 99%

mDia2 formin selectively interacts with catenins and not E-cadherin to regulate Adherens Junction formation

Zhang

Pettee

Becker

et al. 2019

Preprint

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“…Intercellular junctions are connected to, and depend on, the F-actin network for proper formation and maintenance (Yonemura, 2017). Given the profound disruption of the actin network in cells expressing CDTa, we assessed the effect of this toxin on the distribution and levels of junctional proteins.…”

Section: Cdta Alters the Distribution Of Rab11 And Key Junctional Promentioning

confidence: 99%

“…Given the profound disruption of the actin network in cells expressing CDTa, we assessed the effect of this toxin on the distribution and levels of junctional proteins. Adherens junctions are a critical part of the structural framework that maintains tissue integrity, by providing lines of cell-to-cell attachment (Yonemura, 2017). They are composed of trans-membrane Cadherins, which form homodimers with cognate Cadherins expressed by neighboring cells.…”

Section: Cdta Alters the Distribution Of Rab11 And Key Junctional Promentioning

confidence: 99%

“…They are composed of trans-membrane Cadherins, which form homodimers with cognate Cadherins expressed by neighboring cells. They also bind to intracellular alpha-Catenins, which serve as a link to actin filaments (Yonemura, 2017;Mè ge and Ishiyama, 2017). We compared alpha-Catenin distribution in control versus CDTa-expressing guts ( Figure 4A).…”

Section: Cdta Alters the Distribution Of Rab11 And Key Junctional Promentioning

confidence: 99%

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A Drosophila Model for Clostridium difficile Toxin CDT Reveals Interactions with Multiple Effector Pathways

et al. 2020

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Clostridium difficile infections (CDIs) cause severe and occasionally life-threatening diarrhea. Hypervirulent strains produce CDT, a toxin that ADP-ribosylates actin monomers and inhibits actin polymerization. We created transgenic Drosophila lines expressing the catalytic subunit CDTa to investigate its interaction with host signaling pathways in vivo. When expressed in the midgut, CDTa reduces body weight and fecal output and compromises survival, suggesting severe impairment of digestive functions. At the cellular level, CDTa induces F-actin network collapse, elimination of the intestinal brush border, and disruption of intercellular junctions. We confirm toxin-dependent redistribution of Rab11 to enterocytes' apical surface and observe suppression of CDTa phenotypes by a Dominant-Negative form of Rab11 or RNAi of the dedicated Rab11GEF Crag (DENND4). We also report that Calmodulin (Cam) is required to mediate CDTa activity. In parallel, chemical inhibition of the Cam/Calcineurin pathway by Cyclosporin A or FK506 also reduces CDTa phenotypes, potentially opening new avenues for treating CDIs.

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“…Cardiomyocytes have at least two distinct actin networks at cell-cell contactsmyofibrils and the cortical cytoskeleton (Li et al, 2019)that must be integrated at AJs. Many actin-binding ligands interact with E-catenin, including vinculin, afadin, ZO-1 and Eplin (Yonemura, 2017). In epithelia, vinculin is recruited to E-catenin in a forcedependent manner and this interaction is thought to be important for reinforcing the E-catenin:actin interaction (le Duc et al, 2010;Yonemura et al, 2010;Kale et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Vinculin anchors contractile actin to the cardiomyocyte adherens junction

Merkel

Raza

et al. 2019

Preprint

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The adherens junction (AJ) couples the actin cytoskeletons of neighboring cells to allow mechanical integration and tissue organization. The physiological demands of intercellular adhesion require that the AJ be responsive to dynamic changes in force while maintaining mechanical load. These demands are tested in the heart, where cardiomyocyte AJs must withstand repeated cycles of actomyosinmediated contractile force. Here we show that force-responsive cardiomyocyte AJs recruit actin-binding ligands to selectively couple actin networks and promote contact maturation. We employed a panel of N-cadherin-E-catenin fusion proteins to rebuild AJs with specific actin linkages in N-cadherin-null cardiomyocytes. In this system, vinculin recruitment was required to rescue myofibril integration and desmosome assembly at nascent contacts. In contrast, loss of vinculin disrupted junction morphology and blocked myofibril integration. Our results identify vinculin as a critical link to contractile actomyosin and offer insight to how actin integration at the AJ is regulated to provide mechanical stability and cellular organization.

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Actin filament association at adherens junctions

Cited by 21 publications

References 64 publications

mDia2 formin selectively interacts with catenins and not E-cadherin to regulate Adherens Junction formation

mDia2 formin selectively interacts with catenins and not E-cadherin to regulate Adherens Junction formation

A Drosophila Model for Clostridium difficile Toxin CDT Reveals Interactions with Multiple Effector Pathways

Vinculin anchors contractile actin to the cardiomyocyte adherens junction

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