The BioGRID | PUBLICATION VIEW

	Biochem. Biophys. Res. Commun. Apr (2000); 270(3):903-9
MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures.
Dobrosotskaya IY, James GL
Graduate Program in Cell Regulation, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75235, USA. irinadobro@hotmail.com
Abstract: The family of membrane-associated guanylate kinases (MAGUK) comprises peripheral membrane proteins involved in the formation of specialized cell-cell junctions. MAGUK proteins possess a conserved domain composition, containing PDZ, guanylate kinase, and SH3 or WW domains. MAGI-1 is a recently identified member of the MAGUK protein family. Three splice variantsof MAGI-1 have been characterized to date, including MAGI-1a, -1b, and -1c. MAGI-1b is predominantly associated with the crude membrane fraction. Here we show that the fifth PDZ domain of MAGI-1b is essential for membrane localization. We have also identified beta-catenin as a potential ligand for this PDZ domain. MAGI-1b forms complexes with beta-catenin and E-cadherin during the formation of cell-cell junctions in MDCK cells. In agreement with this observation, a significant portion of a GFP fusion of MAGI-1b localizes to the basolateral membrane of polarized MDCK cells.
[PUBMED: 10772923]