Upon processing in the endoplasmic reticulum (ER), pro-CDH1, bound to beta-catenin (CTNNB1), translocates to the Golgi apparatus for further processing. Recombinant CDH1 mutants that do not undergo proper N-glycosylation on asparagine residues in the ER do not translocate to Golgi, but are retained in the ER (Zhou et al. 2008). Similarly, canine CDH1 mutants that cannot bind to CTNNB1 (beta-catenin) are mainly retained in the ER and not detectable in Golgi (Chen et al. 1999). RHO GTPase activator protein (GAP) ARHGAP32 (also known as RICS) forms a complex with CTNNB1-bound CDH1 (Okabe et al. 2003) and facilitates transport of the CDH1:CTNNB1 complex from the ER to Golgi (Nakamura et al. 2008).
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, so that the CDH1:JUP complex would traffic from the ER to Golgi. Different cell types show different ratios of CDH1:CTNNB1 and CDH1:JUP complexes (Butz and Kemler 1994).
Zhou, F, Su, J, Fu, L, Yang, Y, Zhang, L, Wang, L, Zhao, H, Zhang, D, Li, Z, Zha, X
Zhu, W, Leber, B, Andrews, DW
Nakamura, T, Hayashi, T, Nasu-Nishimura, Y, Sakaue, F, Morishita, Y, Okabe, T, Ohwada, S, Matsuura, K, Akiyama, T
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