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Reconstitution of the full transmembrane cadherin-catenin complex.

Authors :
Maker, Allison
Gumbiner, Barry M.
Source :
Protein Expression & Purification. May2022, Vol. 193, pN.PAG-N.PAG. 1p.
Publication Year :
2022

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10465928
Volume :
193
Database :
Academic Search Index
Journal :
Protein Expression & Purification
Publication Type :
Academic Journal
Accession number :
155206261
Full Text :
https://doi.org/10.1016/j.pep.2022.106056