Identification of mNET1 as a candidate ligand for the first PDZ domain of MAGI-1.
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.
Dobrosotskaya
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Graduate Program in Cell Regulation, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA. irinadobro@hotmail.com
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D018076:DNA, Complementary; D020662:Guanine Nucleotide Exchange Factors / Q000737:chemistry / Q000378:metabolism*; D051528:Guanylate Kinases; D006801:Humans; D051379:Mice; D009703:Nucleoside-Phosphate Kinase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011233:Precipitin Tests; D020798:Two-Hybrid System Techniques
D018076:DNA, Complementary; D020662:Guanine Nucleotide Exchange Factors; D009703:Nucleoside-Phosphate Kinase; D051528:Guanylate Kinases