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© The Rockefeller University Press, 0021-9525/1998//1433 $5.00
The Journal of Cell Biology, Volume 141, Number 6, , 1998 1433-1448

Articles

Differential Nuclear Translocation and Transactivation Potential of β-Catenin and Plakoglobin



Inbal Simcha, Michael Shtutman, Daniela Salomon, Jacob Zhurinsky, Einat Sadot, Benjamin Geiger, and Avri Ben-Ze'ev

Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel

β-Catenin and plakoglobin are homologous proteins that function in cell adhesion by linking cadherins to the cytoskeleton and in signaling by transactivation together with lymphoid-enhancing binding/T cell (LEF/TCF) transcription factors. Here we compared the nuclear translocation and transactivation abilities of β-catenin and plakoglobin in mammalian cells. Overexpression of each of the two proteins in MDCK cells resulted in nuclear translocation and formation of nuclear aggregates. The β-catenin-containing nuclear structures also contained LEF-1 and vinculin, while plakoglobin was inefficient in recruiting these molecules, suggesting that its interaction with LEF-1 and vinculin is significantly weaker. Moreover, transfection of LEF-1 translocated endogenous β-catenin, but not plakoglobin to the nucleus. Chimeras consisting of Gal4 DNA-binding domain and the transactivation domains of either plakoglobin or β-catenin were equally potent in transactivating a Gal4-responsive reporter, whereas activation of LEF-1– responsive transcription was significantly higher with β-catenin. Overexpression of wild-type plakoglobin or mutant β-catenin lacking the transactivation domain induced accumulation of the endogenous β-catenin in the nucleus and LEF-1–responsive transactivation. It is further shown that the constitutive β-catenin–dependent transactivation in SW480 colon carcinoma cells and its nuclear localization can be inhibited by overexpressing N-cadherin or {alpha}-catenin. The results indicate that (a) plakoglobin and β-catenin differ in their nuclear translocation and complexing with LEF-1 and vinculin; (b) LEF-1–dependent transactivation is preferentially driven by β-catenin; and (c) the cytoplasmic partners of β-catenin, cadherin and {alpha}-catenin, can sequester it to the cytoplasm and inhibit its transcriptional activity.

Abbreviations used in this paper: aa, amino acid(s); APC, adenomatous polyposis coli; DBD, DNA-binding domain; HA, hemagglutinin; LEF, lymphoid-enhancing binding factor; TCF, T cell factor; VSV, vesicular stomatitis virus; wt, wild-type.

Address all correspondence to: Avri Ben-Ze'ev, Department of Molecular Cell Biology, Weizman Institute of Science, Rehovot 76100, Israel. Tel.: (972) 8-934-2422. Fax: (972) 8-934-4125. E-mail: lgbenzev{at}weizmann.weizmann.ac.il


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