title: PDZ domain proteins: scaffolds for signaling complexes.
abstract: InaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins at the membrane via its five PDZ domains, enhancing speed and efficiency of vision. Extensive conservation of PDZ domains suggests that these motifs have a general role in organizing diverse signaling complexes.
authors.affiliation: Howard Hughes Medical Institute, Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-9041, USA. rama@chop.swmed.edu
authors.forename: R
authors.initials: R
authors.lastname: Ranganathan
authors.forename: E M
authors.initials: EM
authors.lastname: Ross
mesh_terms: D000818:Animals; D001665:Binding Sites; D015220:Calcium Channels / Q000378:metabolism; D004330:Drosophila; D029721:Drosophila Proteins; D005136:Eye Proteins / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism; D017956:Photoreceptor Cells, Invertebrate / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism; D015398:Signal Transduction; D050052:TRPC Cation Channels; D010738:Type C Phospholipases / Q000378:metabolism
chemical_list: D015220:Calcium Channels; D029721:Drosophila Proteins; D005136:Eye Proteins; D050052:TRPC Cation Channels; C091568:inaD protein, Drosophila; C096351:transient receptor potential cation channel, subfamily C, member 1; D011493:Protein Kinase C; D010738:Type C Phospholipases; D019204:GTP-Binding Proteins