Cadherin is a well-known cell-cell adhesion molecule, and it binds to β-catenin, which in turn binds to α-catenin. However, little is known about the regulatory mechanism underlying the cadherin-mediated cell-cell adhesion. Here we purified two novel β-catenin-interacting proteins with molecular masses of 180 kDa (p180) and 150 kDa (p150) from bovine brain cytosol by using glutathione S-transferase (GST)-β-catenin affinity column chromatography. Mass spectral analysis revealed p180 to be identical to KIAA0313 which has a putative Rap1 guanine nucleotide exchange factor (GEF) domain and p150 to be the same as KIAA0705 which has a high degree of sequence similarity to the synaptic scaffolding molecule (S-SCAM), which binds β-catenin and KIAA0313 in the yeast two-hybrid system and overlay assay, respectively. β-Catenin was coimmunoprecipitated with KIAA0313 in Madin-Darby canine kidney II (MDCKII) cells, bovine brain cytosol, and EL cells. KIAA0313 and β-catenin were partly colocalized at sites of cell-cell contact in MDCKII cells. Taken together, our data suggest that KIAA0313 associates with β-catenin through KIAA0705 in vivo at sites of cell-cell contact. (C) 2000 Academic Press.
|ジャーナル||Biochemical and Biophysical Research Communications|
|出版ステータス||Published - 05-07-2000|
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