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Biochem Biophys Res Commun. 2008 Apr 4;368(2):285-91. doi: 10.1016/j.bbrc.2008.01.088. Epub 2008 Jan 28.

Wnt7a interaction with Fzd5 and detection of signaling activation using a split eGFP.

Author information

1
Department of Integrative Biology and Pharmacology, University of Texas Health Science Center Houston, 6431 Fannin Street, Houston, TX 77030, USA.

Abstract

Wnts are secreted glycoproteins that regulate important cellular processes including proliferation, differentiation, and cell fate. In the beta-catenin/canonical pathway, Wnt interacts with Fzd receptors to inhibit degradation of beta-catenin and promote its translocation into the nucleus where it regulates transcription of a number of genes. Dysregulation of this pathway has been attributed to a host of diseases including cancer. As a result, components of the beta-catenin/canonical pathway have been gaining recognition as promising targets for the discovery of novel therapeutic agents. Here, we show, using an ELISA-based protein-protein binding assay that purified Wnt7a binds to the extracellular cysteine-rich domain of Fzd5 in the nanomolar range. We have developed a novel split eGFP complementation assay to visually detect Wnt7a-Fzd5 interactions and subsequent pathway activation in cells. These biological tools could help lead to a better understanding of Wnt-Fzd interactions and the identification of new modulators of Wnt signaling.

PMID:
18230341
PMCID:
PMC2277340
DOI:
10.1016/j.bbrc.2008.01.088
[Indexed for MEDLINE]
Free PMC Article

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