title: The transient receptor potential protein (Trp), a putative store-operated Ca2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, InaC and InaD.
abstract: The transient receptor potential protein (Trp) is a putative capacitative Ca2+ entry channel present in fly photoreceptors, which use the inositol 1,4,5-trisphosphate (InsP3) signaling pathway for phototransduction. By immunoprecipitation studies, we find that Trp is associated into a multiprotein complex with the norpA-encoded phospholipase C, an eye-specific protein kinase C (InaC) and with the InaD protein (InaD). InaD is a putative substrate of InaC and contains two PDZ repeats, putative protein-protein interaction domains. These proteins are present in the photoreceptor membrane at about equimolar ratios. The Trp homolog analyzed here is isolated together with NorpA, InaC and InaD from blowfly (Calliphora) photoreceptors. Compared to Drosophila Trp, the Calliphora Trp homolog displays 77% amino acid identity. The highest sequence conservation is found in the region that contains the putative transmembrane domains S1-S6 (91% amino acid identity). As investigated by immunogold labeling with specific antibodies directed against Trp and InaD, the Trp signaling complex is located in the microvillar membranes of the photoreceptor cells. The spatial distribution of the signaling complex argues against a direct conformational coupling of Trp to an InsP3 receptor supposed to be present in the membrane of internal photoreceptor Ca2+ stores. It is suggested that the organization of signal transducing proteins into a multiprotein complex provides the structural basis for an efficient and fast activation and regulation of Ca2+ entry through the Trp channel.
authors.affiliation: Zoological Institute I, University of Karlsruhe, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Huber
authors.forename: P
authors.initials: P
authors.lastname: Sander
authors.forename: A
authors.initials: A
authors.lastname: Gobert
authors.forename: M
authors.initials: M
authors.lastname: Bähner
authors.forename: R
authors.initials: R
authors.lastname: Hermann
authors.forename: R
authors.initials: R
authors.lastname: Paulsen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015220:Calcium Channels / Q000235:genetics / Q000378:metabolism*; D004175:Diptera / Q000235:genetics; D029721:Drosophila Proteins; D005136:Eye Proteins / Q000737:chemistry / Q000378:metabolism*; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000378:metabolism*; D054799:Phospholipase C beta; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D010786:Photoreceptor Cells / Q000378:metabolism*; D011485:Protein Binding; D011493:Protein Kinase C / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013347:Subcellular Fractions / Q000378:metabolism; D050051:Transient Receptor Potential Channels; D010738:Type C Phospholipases
chemical_list: D015220:Calcium Channels; D029721:Drosophila Proteins; D005136:Eye Proteins; D019476:Insect Proteins; D010716:Phosphatidylinositols; D050051:Transient Receptor Potential Channels; C091568:inaD protein, Drosophila; C063169:trp protein, Drosophila; C103744:InaC protein, Drosophila; D011493:Protein Kinase C; D010727:Phosphoric Diester Hydrolases; D010738:Type C Phospholipases; C468371:NorpA protein, Drosophila; D054799:Phospholipase C beta; D043265:Phosphatidylinositol Diacylglycerol-Lyase