CTNNB1, JUP bind CDH1

Stable Identifier
R-HSA-9933194
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
3/5
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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).
Literature References
PubMed ID Title Journal Year
9700170 Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation

Chitaev, NA, Troyanovsky, SM

J Cell Biol 1998
11689440 Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis

Zhu, W, Leber, B, Andrews, DW

EMBO J 2001
7982500 Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion

Butz, S, Kemler, R

FEBS Lett 1994
18937087 E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/Golgi compartments

Curtis, MW, Johnson, KR, Wheelock, MJ

Cell Commun Adhes 2008
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