Dynamic interactions between E-cadherin and Ankyrin-G mediate epithelial cell polarity maintenance

Chao Kong, Xiaozhan Qu, Mingming Liu, Weiya Xu, Da Chen, Yanshen Zhang, Shan Zhang, Feng Zhu, Zhenbang Liu, Jianchao Li, Chengdong Huang () and Chao Wang ()
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Chao Kong: University of Science and Technology of China
Xiaozhan Qu: University of Science and Technology of China
Mingming Liu: University of Science and Technology of China
Weiya Xu: University of Science and Technology of China
Da Chen: University of Science and Technology of China
Yanshen Zhang: University of Science and Technology of China
Shan Zhang: University of Science and Technology of China
Feng Zhu: University of Science and Technology of China
Zhenbang Liu: University of Science and Technology of China
Jianchao Li: South China University of Technology
Chengdong Huang: University of Science and Technology of China
Chao Wang: University of Science and Technology of China

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract E-cadherin is an essential cell‒cell adhesion protein that mediates canonical cadherin-catenin complex formation in epithelial lateral membranes. Ankyrin-G (AnkG), a scaffold protein linking membrane proteins to the spectrin-based cytoskeleton, coordinates with E-cadherin to maintain epithelial cell polarity. However, the molecular mechanisms governing this complex formation and its relationships with the cadherin-catenin complex remain elusive. Here, we report that AnkG employs a promiscuous manner to encapsulate three discrete sites of E-cadherin by the same region, a dynamic mechanism that is distinct from the canonical 1:1 molar ratio previously described for other AnkG or E-cadherin-mediated complexes. Moreover, we demonstrate that AnkG-binding-deficient E-cadherin exhibited defective accumulation at the lateral membranes and show that disruption of interactions resulted in cell polarity malfunction. Finally, we demonstrate that E-cadherin is capable of simultaneously anchoring to AnkG and β-catenin, providing mechanistic insights into the functional orchestration of the ankyrin-spectrin complex with the cadherin-catenin complex. Collectively, our results show that complex formation between E-cadherin and AnkG is dynamic, which enables the maintenance of epithelial cell polarity by ensuring faithful targeting of the adhesion molecule-scaffold protein complex, thus providing molecular mechanisms for essential E-cadherin-mediated complex assembly at cell‒cell junctions.

Date: 2023
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DOI: 10.1038/s41467-023-42628-1

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