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Roura, S. et al.

Roura, Martínez, Piedra, Miravet, García de Herreros, Duñach,

APC 3 x 15 beta-catenin- binding domain potentiates beta-catenin association to TBP and upregulates TCF-4 transcriptional activity.

Beta-catenin plays a dual role as a regulatory component of adherens junctions and as a transcriptional cofactor. The nuclear activity of this protein is controlled by adenomatous polyposis coli (APC) protein. We have analyzed the effect on beta-catenin-dependent transcription of a beta-catenin binding domain present in APC, consisting in three 15-amino acid repeats (APC 3 x 15). Association of this fragment prevents the interaction of beta-catenin with E-cadherin but not with TCF-4. Transfection of this fragment to several cell lines increases the transcriptional activity of the beta-catenin-TCF-4 complex and promotes the translocation of beta-catenin to the nucleus. Moreover, previous binding of APC 3 x 15 facilitates the association of beta-catenin to the TATA box-associated protein. Therefore, APC 3 x 15 domain plays a positive role in the control of transcriptional activity of beta-catenin-TCF-4 and can contribute to explain the role of the truncated forms of APC in colon tumorigenesis.[1]

References

APC 3 x 15 beta-catenin-binding domain potentiates beta-catenin association to TBP and upregulates TCF-4 transcriptional activity. Roura, S., Martínez, D., Piedra, J., Miravet, S., García de Herreros, A., Duñach, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]

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