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CTNNB1 (beta-catenin) was shown to associate with the cyt...
| Class:Id | Summation:9933204 |
|---|---|
| _displayName | CTNNB1 (beta-catenin) was shown to associate with the cyt... |
| _timestamp | 2025-01-22 02:24:53 |
| created | [InstanceEdit:9933205] Orlic-Milacic, Marija, 2024-12-27 |
| literatureReference | [LiteratureReference:9933207] E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/Golgi compartments [LiteratureReference:9768732] Coupling assembly of the E-cadherin/beta-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells [LiteratureReference:9933208] Contextual binding of p120ctn to E-cadherin at the basolateral plasma membrane in polarized epithelia [LiteratureReference:9933683] Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion [LiteratureReference:9816226] Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis [LiteratureReference:9762154] Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation [LiteratureReference:9762176] Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion [LiteratureReference:9934388] Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes [LiteratureReference:9934393] The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species [LiteratureReference:9762171] Assembly of the cadherin-catenin complex in vitro with recombinant proteins |
| modified | [InstanceEdit:9933301] Orlic-Milacic, Marija, 2024-12-28 [InstanceEdit:9933374] Orlic-Milacic, Marija, 2024-12-29 [InstanceEdit:9933685] Orlic-Milacic, Marija, 2025-01-03 [InstanceEdit:9934390] Orlic-Milacic, Marija, 2025-01-08 [InstanceEdit:9934391] Orlic-Milacic, Marija, 2025-01-08 [InstanceEdit:9934395] Orlic-Milacic, Marija, 2025-01-08 [InstanceEdit:9934407] Orlic-Milacic, Marija, 2025-01-08 [InstanceEdit:9936219] Orlic-Milacic, Marija, 2025-01-22 |
| text | CTNNB1 (beta-catenin) was shown to associate with the cytoplasmic tail of CDH1 (E-cadherin) during CDH1 processing in the endoplasmic reticulum (ER) in both canine MDCK cell line (Chen et al. 1999; Miranda et al. 2003) and human cell lines (Curtis et al. 2008). Based on the study of canine CDH1 mutants containing internal deletions in the cytoplasmic tail, the ability of CDH1 to localize to the basolateral plasma membrane correlates with its ability to bind to CTNNB1 (Chen et al. 1999). The study using recombinant human CDH1 overexpressed in human cell lines showed that, besides CTNNB1, CTNNA1 (alpha-catenin) and CTNND1 (delta-catenin) also associate with the pro-CDH1 during its transition through the ER and Golgi (Curtis et al. 2008). Using recombinant human CDH1 expressed in canine MDCK cells, however, it was shown that the association between CDH1 and CTNND1, unlike the association between CDH1 and CTNNB1, occurs at the plasma membrane and not during trafficking of CDH1 through the ER (Miranda et al. 2003). Phosphorylation of the cytosolic tail of CDH1, likely by the Casein Kinase II (CK2) complex, increases the binding of CTNNB1 to CDH1 (Lickert et al. 2000). JUP (commonly known as Plakoglobin or gamma-catenin) was first reported to associate with CDH1 in the mouse NIH3T3 cell line (Ozawa et al. 1989), and then in the canine MDCK cell line (Reynolds et al. 1994). In human cancer cell line A431, it was shown that binding of JUP to CDH1 is mutually exclusive with CTNNB1 binding to CDH1 (Butz and Kemler 1994; Chitaev and Troyanovsky 1998). While the role of JUP in CDH1 posttranslational processing has not been studied, it was found, in a study using human breast cancer cell lines, that O-glycosylation of the cytosolic tail of CDH1 in apoptosis, which prevents its trafficking to the plasma membrane, does not interfere with its binding to JUP (Zhu et al. 2001), suggesting that JUP associates with CDH1 at a similar point as CTNNB1. Different cell types show different ratios of CDH1:CTNNB1 and CDH1:JUP complexes (Butz and Kemler 1994). The cytosolic tail of CDH1 has a higher affinity for CTNNB1 than JUP (Aberle et al. 1994). |
| (summation) | [Reaction:9933194] CTNNB1, JUP bind CDH1 [Homo sapiens] |
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CTNNB1 (beta-catenin) was shown to associate with the cyt... (9933204)
