+検索条件
-Structure paper
| タイトル | Reconstitution of the full transmembrane cadherin-catenin complex. |
|---|---|
| ジャーナル・号・ページ | Protein Expr Purif, Vol. 193, Page 106056, Year 2022 |
| 掲載日 | 2022年1月18日 |
著者 | Allison Maker / Barry M Gumbiner / ![]() |
| PubMed 要旨 | The dynamic regulation of epithelial adherens junctions relies on all components of the E-cadherin-catenin complex. Previously, the complexes have been partially reconstituted and composed only of α- ...The dynamic regulation of epithelial adherens junctions relies on all components of the E-cadherin-catenin complex. Previously, the complexes have been partially reconstituted and composed only of α-catenin, β-catenin, and the E-cadherin cytoplasmic domain. However, p120-catenin and the full-length E-cadherin including the extracellular, transmembrane, and intra-cellular domains are vital to the understanding of the relationship between extracellular adhesion and intracellular signaling. Here, we reconstitute the complete and full-length cadherin-catenin complex, including full-length E-cadherin, α-catenin, β-catenin, and p120-catenin, into nanodiscs. We are able to observe the cadherin in nanodiscs by cryo-EM. We also reconstitute α-catenin, β-catenin, and p120-catenin with the E-cadherin cytoplasmic tail alone in order to analyze the affinities of their binding interactions. We find that p120-catenin does not associate strongly with α- or β-catenin and binds much more transiently to the cadherin cytoplasmic tail than does β-catenin. Overall, this work creates many new possibilities for biochemical studies understanding transmembrane signaling of cadherins and the role of p120-catenin in adhesion activation. |
リンク | Protein Expr Purif / PubMed:35063654 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 4.56 - 6.11 Å |
| 構造データ | ![]() EMDB-25883: ![]() EMDB-25884: ![]() EMDB-25886: ![]() EMDB-25892: |
| 由来 |
|
ムービー
コントローラー
構造ビューア
万見文献について



著者
リンク



Homo sapiens (ヒト)
