P120 catenin potentiates constitutive E-cadherin dimerization at the plasma membrane and regulates trans binding

Vu, Vinh; Light, Taylor P.; Sullivan, Brendan G.; Greiner, Diana; Hristova, Kalina; Leckband, Deborah

doi:10.1016/j.cub.2021.04.061

Cited by 24 publications

(19 citation statements)

References 81 publications

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“…Recently, researchers unraveled an unexpected mechanism of cadherin oligomerization in cells by using FRET microscopy ( Vu et al, 2021 ). It was thought that only extracellular domain interactions were responsible for lateral ( cis ) cadherin oligomerization ( Singh et al, 2017 ; Thompson et al, 2020 ).…”

Section: Light-based Microscopy Techniquesmentioning

confidence: 99%

“…Disrupted p120 catenin binding to E-cadherin further showed that this reduced cadherin trans binding affinity and cell adhesion. This implies that both extra- and intracellular cadherin domains play a role in the cadherin clustering and adhesion with p120 catenin as a key role ( Vu et al, 2021 ). Another research study also used FRET to look at the cis and trans interactions, and their cooperativity, of cadherin transmembrane proteins.…”

Section: Light-based Microscopy Techniquesmentioning

confidence: 99%

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Microscopic Visualization of Cell-Cell Adhesion Complexes at Micro and Nanoscale

Vanslembrouck

Chen

Larabell

et al. 2022

Front. Cell Dev. Biol.

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Considerable progress has been made in our knowledge of the morphological and functional varieties of anchoring junctions. Cell-cell adhesion contacts consist of discrete junctional structures responsible for the mechanical coupling of cytoskeletons and allow the transmission of mechanical signals across the cell collective. The three main adhesion complexes are adherens junctions, tight junctions, and desmosomes. Microscopy has played a fundamental role in understanding these adhesion complexes on different levels in both physiological and pathological conditions. In this review, we discuss the main light and electron microscopy techniques used to unravel the structure and composition of the three cell-cell contacts in epithelial and endothelial cells. It functions as a guide to pick the appropriate imaging technique(s) for the adhesion complexes of interest. We also point out the latest techniques that have emerged. At the end, we discuss the problems investigators encounter during their cell-cell adhesion research using microscopic techniques.

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Section: Light-based Microscopy Techniquesmentioning

confidence: 99%

Section: Light-based Microscopy Techniquesmentioning

confidence: 99%

Microscopic Visualization of Cell-Cell Adhesion Complexes at Micro and Nanoscale

Vanslembrouck

Chen

Larabell

et al. 2022

Front. Cell Dev. Biol.

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“…The ectodomain requirement differs from evidence that the transmembrane domain of vascular endothelial cadherin mediates binding to vascular endothelial growth factor receptors 2/3 ( 68 ). Future FSI-FRET measurements will identify regions of EGFR and E-cadherin that mediate heterocomplex formation and establish whether E-cadherin dimers ( 52 , 69 ) are required.…”

Section: Discussionmentioning

confidence: 99%

Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor–dependent signaling

Sullivan

Light

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

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Increased intercellular tension is associated with enhanced cell proliferation and tissue growth. Here, we present evidence for a force-transduction mechanism that links mechanical perturbations of epithelial (E)-cadherin (CDH1) receptors to the force-dependent activation of epidermal growth factor receptor (EGFR, ERBB1)—a key regulator of cell proliferation. Here, coimmunoprecipitation studies first show that E-cadherin and EGFR form complexes at the plasma membrane that are disrupted by either epidermal growth factor (EGF) or increased tension on homophilic E-cadherin bonds. Although force on E-cadherin bonds disrupts the complex in the absence of EGF, soluble EGF is required to mechanically activate EGFR at cadherin adhesions. Fully quantified spectral imaging fluorescence resonance energy transfer further revealed that E-cadherin and EGFR directly associate to form a heterotrimeric complex of two cadherins and one EGFR protein. Together, these results support a model in which the tugging forces on homophilic E-cadherin bonds trigger force-activated signaling by releasing EGFR monomers to dimerize, bind EGF ligand, and signal. These findings reveal the initial steps in E-cadherin–mediated force transduction that directly link intercellular force fluctuations to the activation of growth regulatory signaling cascades.

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“…The JMD of E-cadherin also contains sites for tyrosine phosphorylation-mediated ubiquitination by the E3 ubiquitin ligase Hakai (encoded by the CBLL1 gene), which targets E-cadherin for endocytosis and proteasomal or lysosomal degradation [ 93 , 94 ]. Finally, the binding of E-cadherin to p120 has been found to be crucial in the constitutive dimerization of E-cadherin, which is instrumental for the formation of AJs [ 95 ]. Interestingly, the degradation of E-cadherin promoted by phosphorylation of the JMD domain is thought to be an early event that precedes transcriptional inhibition of CDH1 during EMT [ 96 ].…”

Section: Cell-to-cell Contacts Adherens Junctions and Emtmentioning

confidence: 99%

The Autophagic Route of E-Cadherin and Cell Adhesion Molecules in Cancer Progression

Santarosa

Maestro

2021

Cancers

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Cell-to-cell adhesion is a key element in epithelial tissue integrity and homeostasis during embryogenesis, response to damage, and differentiation. Loss of cell adhesion and gain of mesenchymal features, a phenomenon known as epithelial to mesenchymal transition (EMT), are essential steps in cancer progression. Interestingly, downregulation or degradation by endocytosis of epithelial adhesion molecules (e.g., E-cadherin) associates with EMT and promotes cell migration. Autophagy is a physiological intracellular degradation and recycling process. In cancer, it is thought to exert a tumor suppressive role in the early phases of cell transformation but, once cells have gained a fully transformed phenotype, autophagy may fuel malignant progression by promoting EMT and conferring drug resistance. In this review, we discuss the crosstalk between autophagy, EMT, and turnover of epithelial cell adhesion molecules, with particular attention to E-cadherin.

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P120 catenin potentiates constitutive E-cadherin dimerization at the plasma membrane and regulates trans binding

Cited by 24 publications

References 81 publications

Microscopic Visualization of Cell-Cell Adhesion Complexes at Micro and Nanoscale

Microscopic Visualization of Cell-Cell Adhesion Complexes at Micro and Nanoscale

Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor–dependent signaling

The Autophagic Route of E-Cadherin and Cell Adhesion Molecules in Cancer Progression

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