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Biochem. Biophys. Res. Commun. May (2001); 283(4):969-75
Identification of mNET1 as a candidate ligand for the first PDZ domain of MAGI-1.
Dobrosotskaya IY
Graduate Program in Cell Regulation, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA. irinadobro@hotmail.com
Abstract: This paper reports the identification of a Rho family nucleotide exchange factor termed mNET1 as a candidate-interacting partner for the first PDZ domain of MAGI-1, a membrane-associated guanylate kinase with inverted arrangement of protein-protein interacting modules. mNET1 was identified in a yeast two-hybrid screen and has a consensus tripeptide for PDZ domain binding at its extreme carboxy-terminus. In addition to this sequence, a cluster of basic residues located near the carboxy terminus is essential for the binding. The interaction of the first PDZ domain of MAGI-1with mNET1 was documented using a variety of biochemical methods.
[PUBMED: 11350080] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
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BioGRID: A General Repository for Interaction Datasets.
Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.