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	Biochem. Biophys. Res. Commun. Jun (1998); 247(3):597-604
Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1.
Shiratsuchi T, Futamura M, Oda K, Nishimori H, Nakamura Y, Tokino T
Laboratory of Molecular Medicine, University of Tokyo, Japan.
Abstract: Brain-specific angiogenesis inhibitor 1 (BAI1), which is a p53-target gene specifically expressed in brain, encodes a seven-span transmembrane protein. Using a two-hybrid system, we isolated a cDNA that encodes a protein, named BAP1 (BAI1-associated protein), which interacts with the cytoplasmic region of BAI1. BAP1 is a novel member of the MAGUK (membrane-associated guanylate kinase homologue) family; it possesses a guanylate kinase domain, WW domains, and multiple PDZ domains. Interaction between BAI1 and BAP1 was mediated by a QTEV motif in the carboxy-terminal region of BAI1 and PDZ domains of BAP1. By immunocytochemical analysis of COS-7 cells transfected with BAI1 and BAP1, both products were co-localized at the cytoplasmic membrane, especially at cell-cell junctions. Cells transfected with BAI1 formed filopodia-like cytoplasmic extensions. These results suggest that BAI1 and BAP1 might be involved in cell adhesion and signal transduction in brain.
[PUBMED: 9647739]