Reconstitution of the full transmembrane cadherin-catenin complex.
Adhesion
Catenin
E-Cadherin
Nanodiscs
Protein complexes
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
received:
14
12
2021
accepted:
13
01
2022
pubmed:
23
1
2022
medline:
8
4
2022
entrez:
22
1
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35063654
pii: S1046-5928(22)00013-4
doi: 10.1016/j.pep.2022.106056
pmc: PMC9487826
mid: NIHMS1773899
pii:
doi:
Substances chimiques
Cadherins
0
Catenins
0
Phosphoproteins
0
beta Catenin
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
106056Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM122467
Pays : United States
Organisme : NIH HHS
ID : S10 OD023476
Pays : United States
Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.
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