ERBIN associates with p0071, an armadillo protein, at cell‐cell junctions of epithelial cells

Abstract

Summary Figure Working model for the ERBIN–p0071 interaction at cell‐cell adhesions. ERBIN is associated with p0071 at adherens junctions and desmosomes. p0071 is thought to interact with classic cadherins or desmosomal cadherins (Hatzfeld 1999). The subcellular localization of ERBIN may be regulated by the Rho family and other signals controlling cell polarity. Background: ERBIN, an ErbB2 receptor‐interacting protein, belongs to a recently described family of proteins termed the LAP [leucine‐rich repeats and PSD‐95/dLg‐A/ZO‐1 (PDZ) domains] family which has essential roles in establishment of cell polarity. Results: To identify new ERBIN‐binding proteins, we screened a yeast two‐hybrid library, using the carboxyl‐terminal fragment of ERBIN containing PDZ domain as the bait, and we isolated p0071 (also called plakophilin‐4) as an ERBIN‐interacting protein. p0071 is a member of the p120 catenin family, which are defined as proteins with 10 armadillo repeats, and localizes along the cell‐cell border. The ERBIN PDZ domain binds the COOH‐terminus of p0071 containing the PDZ domain‐binding sequence. Endogenous ERBIN was co‐immunoprecipitated with p0071. In fully polarized Madin–Darby canine kidney (MDCK) cells, ERBIN co‐localized largely with β‐catenin and partly with desmoplakin along the lateral plasma membrane domain. At these cell‐cell contact regions, ERBIN co‐localizes with p0071. Over‐expression of the dominant active forms of Cdc42, Rac1 or RhoA, Rho family small GTPases, resulted in a marked accumulation of ERBIN at the cell‐cell contacts of MDCK and HeLa cells. Conclusion: These results show that ERBIN interacts in vivo with p0071 and that it may be involved in the organization of adherens junctions and the desmosomes of epithelia. In addition, we demonstrated that the subcellular localization of ERBIN might be regulated by Rho family small GTPases.

Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells

“…Jaulin-Bastard et al (2002) explored ERBIN interactors and obtained p0071 and later Izawa et al (2002b) reported the same interaction. It was also reported that the overexpressed carboxyl-terminus of p0071 disrupts the integrity of cell junctions in HeLa cells.…”

“…AIPC transcript and protein are up-regulated in prostate tumor cells, suggesting that PAPIN may be involved in the regulation of cell proliferation and polarity. Furthermore, a very recent report has revealed that p0071 interacts with ERBIN, a member of the LAP family (Borg et al, 2000;Bryant and Huwe, 2000;Jaulin-Bastard et al, 2002;Izawa et al, 2002b). ERBIN has the leucine-rich repeat in the N-terminal region and one PDZ domain in the carboxyl-terminal region, which binds to p0071.…”

Anchoring Junctions As Drug Targets: Role in Contraceptive Development

“…In terms of protein-protein interactions, p0071 has been shown to associate with desmocollin 3a , desmoplakin (Calkins et al, 2003), plakoglobin , and cadherin (Calkins et al, 2003;Hatzfeld et al, 2003). p0071 also interacts with erbin (Izawa et al, 2002;Jaulin-Bastard et al, 2002) and plakophilin-related armadillo repeat protein-interacting PDZ protein [papin (Deguchi et al, 2000;Ohno et al, 2002)], two PDZ-domain containing proteins that play roles in cell junction dynamics.…”

Scribble protein domain mapping reveals a multistep localization mechanism and domains necessary for establishing cortical polarity

“…More is known about the role of PDZ domains in junctional targeting of LAP proteins. The mammalian LAP proteins Erbin and Densin180 show PDZ-mediated interactions with p120-catenins (Izawa et al, 2002a;Izawa et al, 2002b;Jaulin-Bastard et al, 2002;Laura et al, 2002), and Erbin-catenin p0071 colocalize to adherens junctions and desmosomes in cultured epithelial cells (Izawa et al, 2002b;Jaulin-Bastard et al, 2002). Disruption of Erbin-p0071 interactions leads to aberrant cell morphology and disruption of cell-cell contacts (Jaulin-Bastard et al, 2002).…”