Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo.
about
Drosophila NMNAT maintains neural integrity independent of its NAD synthesis activityInsights into social insects from the genome of the honeybee Apis melliferaIdentification and characterization of a PDZ protein that interacts with activin type II receptorsGlial processes at the Drosophila larval neuromuscular junction match synaptic growthFunctional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpAThe Calliphora rpa mutant lacks the PDZ domain-assembled INAD signalling complex.Two distantly positioned PDZ domains mediate multivalent INAD-phospholipase C interactions essential for G protein-coupled signaling.Scaffolding proteins organize multimolecular protein complexes for sensory signal transduction.Transient receptor potential-like channels are essential for calcium signaling and fluid transport in a Drosophila epithelium.Scaffolding protein INAD regulates deactivation of vision by promoting phosphorylation of transient receptor potential by eye protein kinase C in Drosophila.Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors.Light-induced recruitment of INAD-signaling complexes to detergent-resistant lipid rafts in Drosophila photoreceptors.PDA (prolonged depolarizing afterpotential)-defective mutants: the story of nina's and ina's--pinta and santa maria, too.TRP and the PDZ protein, INAD, form the core complex required for retention of the signalplex in Drosophila photoreceptor cells.Drosophila photoreceptors and signaling mechanisms.Molecular genetics of retinal degeneration: A Drosophila perspective.The regulations of Drosophila phototransduction.Does Ca2+ reach millimolar concentrations after single photon absorption in Drosophila photoreceptor microvilli?Agonist-induced phosphorylation of the serotonin 5-HT2C receptor regulates its interaction with multiple PDZ protein 1.The SOCS box protein STOPS is required for phototransduction through its effects on phospholipase C.Anchoring TRP to the INAD macromolecular complex requires the last 14 residues in its carboxyl terminus.Regulation of Ca2+ release-activated Ca2+ channels by INAD and Ca2+ influx factor.The second PDZ domain of INAD is a type I domain involved in binding to eye protein kinase C. Mutational analysis and naturally occurring variants.The visual G protein of fly photoreceptors interacts with the PDZ domain assembled INAD signaling complex via direct binding of activated Galpha(q) to phospholipase cbeta.Interaction of eye protein kinase C and INAD in Drosophila. Localization of binding domains and electrophysiological characterization of a loss of association in transgenic flies.Specific molecular alterations in the norpA-encoded phospholipase C of Drosophila and their effects on electrophysiological responses in vivo.Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors.Phospholipase C and termination of G-protein-mediated signalling in vivo.
P2860
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P2860
Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Association of INAD with NORPA ...... ila phototransduction in vivo.
@en
type
label
Association of INAD with NORPA ...... ila phototransduction in vivo.
@en
prefLabel
Association of INAD with NORPA ...... ila phototransduction in vivo.
@en
P2093
P2860
P356
P1476
Association of INAD with NORPA ...... ila phototransduction in vivo.
@en
P2093
P2860
P304
12682-12687
P356
10.1073/PNAS.94.23.12682
P407
P577
1997-11-01T00:00:00Z