T. Shiratsuchi et al., CLONING AND CHARACTERIZATION OF BAI-ASSOCIATED PROTEIN-1 - A PDZ DOMAIN-CONTAINING PROTEIN THAT INTERACTS WITH BAI1, Biochemical and biophysical research communications (Print), 247(3), 1998, pp. 597-604
Brain-specific angiogenesis inhibitor 1 (BAI1), which is a p53-target
gene specifically expressed in brain, encodes a seven-span transmembra
ne 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. Intera
ction between BAI1 and BAP1 was mediated by a QTEV motifin the carboxy
-terminal region of BAI1 and PDZ domains of BAP1, By immunocytochemica
l analysis of COS-7 cells transfected with BAI1 and BAP1, both product
s were co-localized at the cytoplasmic membrane, especially at cell-ce
ll junctions. Cells transfected with BAI1 formed filopodia-like cytopl
asmic extensions. These results suggest that BAI1 and BAP1 might be in
volved in cell adhesion and signal transduction in brain. (C) 1998 Aca
demic Press.