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TitleReconstitution of the full transmembrane cadherin-catenin complex.
Journal, issue, pagesProtein Expr Purif, Vol. 193, Page 106056, Year 2022
Publish dateJan 18, 2022
AuthorsAllison Maker / Barry M Gumbiner /
PubMed AbstractThe 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.
External linksProtein Expr Purif / PubMed:35063654 / PubMed Central
MethodsEM (single particle)
Resolution4.56 - 6.11 Å
Structure data

EMDB-25883:
Full-length human E-cadherin bound to 19A11 activating Fab
Method: EM (single particle) / Resolution: 4.83 Å

EMDB-25884:
Full-length human E-cadherin bound to neutral Fab 46H7
Method: EM (single particle) / Resolution: 4.56 Å

EMDB-25886:
Full-length human E-cadherin bound to activating Fab 59D2
Method: EM (single particle) / Resolution: 6.11 Å

EMDB-25892:
Full-length human E-cadherin bound to blocking Fab 67G8
Method: EM (single particle) / Resolution: 5.53 Å

Source
  • Homo sapiens (human)
  • Mus musculus (house mouse)

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