Identification of a novel β-catenin-interacting protein

Aie Kawajiri, Naohiro Itoh, Masaki Fukata, Masato Nakagawa, Masaki Yamaga, Akihiro Iwamatsu, Kozo Kaibuchi

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)712-717
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 05-07-2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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