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Dynamics and functions of E-cadherin complexes in epithelial cell and tissue morphogenesis
Cell–cell adhesion is at the center of structure and dynamics of epithelial tissue. E-cadherin–catenin complexes mediate Ca 2+ -dependent trans- homodimerization and constitute the kernel of adherens junctions. Beyond the basic function of cell–cell adhesion, recent progress sheds light the dynamics...
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Published in: | Marine life science & technology 2023-11, Vol.5 (4), p.585-601 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Cell–cell adhesion is at the center of structure and dynamics of epithelial tissue. E-cadherin–catenin complexes mediate Ca
2+
-dependent
trans-
homodimerization and constitute the kernel of adherens junctions. Beyond the basic function of cell–cell adhesion, recent progress sheds light the dynamics and interwind interactions of individual E-cadherin–catenin complex with E-cadherin superclusters, contractile actomyosin and mechanics of the cortex and adhesion. The nanoscale architecture of E-cadherin complexes together with
cis-
interactions and interactions with cortical actomyosin adjust to junctional tension and mechano-transduction by reinforcement or weakening of specific features of the interactions. Although post-translational modifications such as phosphorylation and glycosylation have been implicated, their role for specific aspects of in E-cadherin function has remained unclear. Here, we provide an overview of the E-cadherin complex in epithelial cell and tissue morphogenesis focusing on nanoscale architectures by super-resolution approaches and post-translational modifications from recent, in particular in vivo, studies. Furthermore, we review the computational modelling in E-cadherin complexes and highlight how computational modelling has contributed to a deeper understanding of the E-cadherin complexes. |
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ISSN: | 2662-1746 2096-6490 2662-1746 |
DOI: | 10.1007/s42995-023-00206-w |