Hakai, an E3-ligase for E-cadherin, stabilizes δ-catenin through Src kinase
| Autor: | Taeyong Ryu, Eunsook Park, Young-Woo Seo, Hridaya Shrestha, Weiye Dai, Hangun Kim, Kwonseop Kim, Keesook Lee, So-Yeon Park, Yongfeng He, Shishli Simkhada |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Delta Catenin Recombinant Fusion Proteins Ubiquitin-Protein Ligases Endocytosis Models Biological Cell Line 03 medical and health sciences 0302 clinical medicine Antigens CD Humans Cell adhesion Glycogen synthase biology Protein Stability Cadherin Cell Membrane Catenins Cell Biology Cadherins Cell biology Ubiquitin ligase src-Family Kinases 030104 developmental biology 030220 oncology & carcinogenesis Catenin biology.protein Gene Deletion Protein Binding Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Cellular Signalling. 31:135-145 |
| ISSN: | 0898-6568 |
| DOI: | 10.1016/j.cellsig.2017.01.009 |
| Popis: | Hakai ubiquitinates and induces endocytosis of the E-cadherin complex; thus, modulating cell adhesion and regulating development of the epithelial-mesenchymal transition of metastasis. Our previous published data show that δ-catenin promotes E-cadherin processing and thereby activates β-catenin-mediated oncogenic signals. Although several published data show the interactions between δ-catenin and E-cadherin and between Hakai and E-cadherin separately, we found no published report on the relationship between δ-catenin and Hakai. In this report, we show Hakai stabilizes δ-catenin regardless of its E3 ligase activity. We show that Hakai and Src increase the stability of δ-catenin synergistically. Hakai stabilizes Src and Src, which in turn, inhibits binding between glycogen synthase kinase-3β and δ-catenin, resulting in less proteosomal degradation of δ-catenin. These results suggest that stabilization of δ-catenin by Hakai is dependent on Src. |
| Databáze: | OpenAIRE |
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