Epithelial cells regulate their contacts with neighboring cells during embryonic development and in disease states such as tumor metastasis. The intercellular adherens junctions (AJs) are specialized subapical structures that function as principle mediators of cell-cell adhesion. Their disassembly correlates with a loss of cell-cell contact and an acquisition of migratory potential. Regulation of the expression of AJ components by gene transcription can dictate the stability of intercellular adhesive contacts, and accruing evidence indicates that the coordinated regulation of cellular processes such as membrane trafficking and cytoskeletal remodeling can also result in the effective dissolution of AJs. Studies of the posttranscriptional mechanisms by which adhesive interactions are regulated in response to growth factors and/or developmental cues have opened new avenues for investigating cell-cell adhesion during development and in disease.
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http://dx.doi.org/10.1016/j.tcb.2004.11.002 | DOI Listing |
Adv Exp Med Biol
January 2025
Cancer Research UK Scotland Centre (Edinburgh), Institute of Genetics & Cancer, University of Edinburgh, Edinburgh, UK.
E-cadherin is a transmembrane protein and central component of adherens junctions (AJs). The extracellular domain of E-cadherin forms homotypic interactions with E-cadherin on adjacent cells, facilitating the formation of cell-cell adhesions, known as AJs, between neighbouring cells. The intracellular domain of E-cadherin interacts with α-, β- and p120-catenins, linking the AJs to the actin cytoskeleton.
View Article and Find Full Text PDFSci Rep
January 2025
Department of Dermatology, Chung-Ang University Hospital, 102, Heukseok-ro, Dongjak-gu, Seoul, Republic of Korea.
Cold atmospheric plasma (CAP) has been utilized in various medical devices using its oxidative nature. Recent studies have provided evidence that CAP can facilitate the delivery of large, hydrophilic molecules through the epidermis to the dermis. On the other hand, a new approach called low-intensity CAP (LICAP) has been developed, allowing the plasma level to be controlled within a subtoxic range, thereby demonstrating various biological benefits without tissue damage.
View Article and Find Full Text PDFArthropod Struct Dev
January 2025
Zoological Museum, University of Kiel, Hegewischstrasse 3, 24105, Kiel, Germany.
The objective of this study is to gain a better understanding of the not well understood egg-transportation mechanisms through the female reproductive systems of crabs. For this, Carcinus maenas was chosen as a model to study the cuticular epithelium underlying the cuticle of the vagina and the ventral seminal receptacle. This cuticular epithelium is investigated by performing histochemical and ultrastructural analyses of the epithelial cells.
View Article and Find Full Text PDFJ Cell Biol
March 2025
Department of Pulmonary Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Epithelial cells can become polyploid upon tissue injury, but mechanosensitive cues that trigger this state are poorly understood. Using an Madin Darby Canine Kidney (MDCK) cell knock-out/reconstitution system, we show that α-catenin mutants that alter force-sensitive binding to F-actin or middle (M)-domain promote cytokinesis failure and binucleation, particularly near epithelial wound-fronts. We identified Leucine Zipper Tumor Suppressor 2 (LZTS2), a factor previously implicated in abscission, as a conformation sensitive proximity partner of α-catenin.
View Article and Find Full Text PDFBiol Open
January 2025
Department of Pulmonary Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Epithelial cell cohesion and barrier function critically depend on α-catenin, an actin-binding protein and essential constituent of cadherin-catenin-based adherens junctions. α-catenin undergoes actomyosin force-dependent unfolding of both actin-binding and middle domains to strongly engage actin filaments and its various effectors; this mechanosensitivity is critical for adherens junction function. We previously showed that α-catenin is highly phosphorylated in an unstructured region that links the mechanosensitive middle and actin-binding domains (known as the P-linker region), but the cellular processes that promote α-catenin phosphorylation have remained elusive.
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