PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9651370-4 1998 We previously demonstrated the direct association between the third PDZ domain of INAD with TRP in addition to the carboxyl-terminal half of INAD with the last three residues of NORPA. Tryptophan 92-95 inactivation no afterpotential D Drosophila melanogaster 82-86 9679151-2 1998 Previous studies show that the PDZ domain containing protein INAD, which functions in Drosophila vision, coordinates a signaling complex by binding directly to the light-sensitive ion channel, TRP, and to phospholipase C (PLC). Tryptophan 193-196 inactivation no afterpotential D Drosophila melanogaster 61-65 9651370-9 1998 Flies homozygous for inaCp209 and InaDp215, a mutation that causes a loss of the INAD-TRP association, were generated. Tryptophan 86-89 inactivation no afterpotential D Drosophila melanogaster 81-85 8630257-3 1996 We report that anti-INAD antibodies coimmunoprecipitate TRP, identified by its electrophoretic mobility, cross reactivity with anti-TRP antibody, and absence in a null allele trp mutant. Tryptophan 56-59 inactivation no afterpotential D Drosophila melanogaster 20-24 9356510-2 1997 Inactivation-no-afterpotential D (INAD) is an adaptor protein containing PDZ domains known to interact with TRP. Tryptophan 108-111 inactivation no afterpotential D Drosophila melanogaster 0-32 9356510-2 1997 Inactivation-no-afterpotential D (INAD) is an adaptor protein containing PDZ domains known to interact with TRP. Tryptophan 108-111 inactivation no afterpotential D Drosophila melanogaster 34-38 9010208-0 1997 Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex. Tryptophan 70-73 inactivation no afterpotential D Drosophila melanogaster 40-44 9010208-2 1997 Here, we show that TRP forms a complex with phospholipase C-beta (NORPA), rhodopsin (RH1), calmodulin, and the PDZ domain containing protein INAD. Tryptophan 19-22 inactivation no afterpotential D Drosophila melanogaster 141-145 9010208-4 1997 We show that in InaD mutant flies, TRP is no longer spatially restricted to its normal subcellular compartment, the rhabdomere. Tryptophan 35-38 inactivation no afterpotential D Drosophila melanogaster 16-20 8630257-3 1996 We report that anti-INAD antibodies coimmunoprecipitate TRP, identified by its electrophoretic mobility, cross reactivity with anti-TRP antibody, and absence in a null allele trp mutant. Tryptophan 175-178 inactivation no afterpotential D Drosophila melanogaster 20-24 26853938-4 2016 The C-terminal 15 residues of TRP are required for the specific interaction with INAD PDZ3. Tryptophan 30-33 inactivation no afterpotential D Drosophila melanogaster 81-85 30458219-4 2019 PLC and TRP are held together in a protein assembly by the scaffold protein INAD. Tryptophan 8-11 inactivation no afterpotential D Drosophila melanogaster 76-80 26853938-5 2016 The INAD PDZ3/TRP peptide complex structure reveals that only the extreme C-terminal Leu of TRP binds to the canonical alphaB/betaB groove of INAD PDZ3. Tryptophan 14-17 inactivation no afterpotential D Drosophila melanogaster 4-8 26853938-5 2016 The INAD PDZ3/TRP peptide complex structure reveals that only the extreme C-terminal Leu of TRP binds to the canonical alphaB/betaB groove of INAD PDZ3. Tryptophan 14-17 inactivation no afterpotential D Drosophila melanogaster 142-146 17689976-5 2007 Mutations affecting INAD and TRP showed that PDZ4 and PDZ5 domains of INAD, as well as the INAD-TRP interaction, are required for translocation of components to DRM rafts. Tryptophan 29-32 inactivation no afterpotential D Drosophila melanogaster 70-74 24961970-5 2014 TRP (but not TRPL) is assembled into multimolecular signalling complexes by a PDZ-domain scaffolding protein (INAD). Tryptophan 0-3 inactivation no afterpotential D Drosophila melanogaster 110-114 20404479-9 2010 TRP has previously been shown to anchor INAD in the rhabdomeres, therefore the independent identification of two trp alleles validates our screen for INAD-GFP localization. Tryptophan 0-3 inactivation no afterpotential D Drosophila melanogaster 40-44 20404479-9 2010 TRP has previously been shown to anchor INAD in the rhabdomeres, therefore the independent identification of two trp alleles validates our screen for INAD-GFP localization. Tryptophan 0-3 inactivation no afterpotential D Drosophila melanogaster 150-154 20404479-9 2010 TRP has previously been shown to anchor INAD in the rhabdomeres, therefore the independent identification of two trp alleles validates our screen for INAD-GFP localization. Tryptophan 113-116 inactivation no afterpotential D Drosophila melanogaster 150-154 17689976-5 2007 Mutations affecting INAD and TRP showed that PDZ4 and PDZ5 domains of INAD, as well as the INAD-TRP interaction, are required for translocation of components to DRM rafts. Tryptophan 29-32 inactivation no afterpotential D Drosophila melanogaster 70-74 15104173-4 2004 Association of target proteins with INAD is required for rapid termination of the photoresponse and for proper localization of signalling proteins, such as TRP. Tryptophan 156-159 inactivation no afterpotential D Drosophila melanogaster 36-40 16914683-4 2006 Moreover, deactivation is regulated by the interaction between INAD and TRP, because abrogation of this interaction in InaD(p215) results in slow deactivation similar to that of inaC(p209) lacking eye-PKC. Tryptophan 72-75 inactivation no afterpotential D Drosophila melanogaster 63-67 16914683-4 2006 Moreover, deactivation is regulated by the interaction between INAD and TRP, because abrogation of this interaction in InaD(p215) results in slow deactivation similar to that of inaC(p209) lacking eye-PKC. Tryptophan 72-75 inactivation no afterpotential D Drosophila melanogaster 119-123 16914683-5 2006 To elucidate the mechanisms whereby eye-PKC modulates deactivation, here we demonstrate that eye-PKC, via tethering to INAD, phosphorylates TRP in vitro. Tryptophan 140-143 inactivation no afterpotential D Drosophila melanogaster 119-123 16914683-7 2006 Furthermore, transgenic expression of modified TRP bearing an Ala substitution leads to slow deactivation of the visual response similar to that of InaD(p215). Tryptophan 47-50 inactivation no afterpotential D Drosophila melanogaster 148-152 16301334-2 2005 Null mutations in trp cause impairment of visual transduction, mislocalization of INAD, and retinal degeneration. Tryptophan 18-21 inactivation no afterpotential D Drosophila melanogaster 82-86 15961416-4 2005 TRP is a member of a supramolecular signalling complex, the signalplex, which includes the PDZ scaffold protein, INAD, and two other core members that remain bound and depend on INAD for localization. Tryptophan 0-3 inactivation no afterpotential D Drosophila melanogaster 113-117 15961416-4 2005 TRP is a member of a supramolecular signalling complex, the signalplex, which includes the PDZ scaffold protein, INAD, and two other core members that remain bound and depend on INAD for localization. Tryptophan 0-3 inactivation no afterpotential D Drosophila melanogaster 178-182 15961416-6 2005 Surprisingly, TRP has non-channel functions, including an anchoring role necessary for retaining INAD in the rhabdomeres. Tryptophan 14-17 inactivation no afterpotential D Drosophila melanogaster 97-101 15695363-12 2005 Finally, a scaffolding component of the TRPL/TRP-signaling complex, INAD, is not expressed in tubules, suggesting that inaD is not essential for TRPL/TRP function in Drosophila tubules. Tryptophan 40-43 inactivation no afterpotential D Drosophila melanogaster 68-72 15104173-5 2004 In addition, TRP is reciprocally required for localizing INAD, indicating that TRP functions as both an ion channel and a molecular anchor. Tryptophan 13-16 inactivation no afterpotential D Drosophila melanogaster 57-61 15104173-5 2004 In addition, TRP is reciprocally required for localizing INAD, indicating that TRP functions as both an ion channel and a molecular anchor. Tryptophan 79-82 inactivation no afterpotential D Drosophila melanogaster 57-61 11150331-4 2001 We find that trp mutants, or transgenic flies expressing inaD alleles that disrupt the interaction between INAD and TRP, cause the mislocalization of the entire transduction complex. Tryptophan 13-16 inactivation no afterpotential D Drosophila melanogaster 107-111 12206995-2 2002 Together with phospholipase Cb and an eye-specific protein kinase C, TRP is tethered to the scaffolding protein INAD, which forms a multimolecular signaling complex. Tryptophan 69-72 inactivation no afterpotential D Drosophila melanogaster 112-116 12206995-5 2002 The situation changed when the PDZ domain protein INAD was coexpressed with TRP. Tryptophan 76-79 inactivation no afterpotential D Drosophila melanogaster 50-54 12206995-7 2002 Suppression of CCE by INAD was not observed when the described interaction was disrupted by mutations in TRP and INAD. Tryptophan 105-108 inactivation no afterpotential D Drosophila melanogaster 22-26 12206995-8 2002 Our data show that apparent activation of TRP by CCE is abolished by INAD. Tryptophan 42-45 inactivation no afterpotential D Drosophila melanogaster 69-73 11150331-4 2001 We find that trp mutants, or transgenic flies expressing inaD alleles that disrupt the interaction between INAD and TRP, cause the mislocalization of the entire transduction complex. Tryptophan 116-119 inactivation no afterpotential D Drosophila melanogaster 57-61 11150331-5 2001 The INAD-TRP interaction is not required for targeting but rather for anchoring of complexes, because INAD and TRP can be targeted independently of each other. Tryptophan 9-12 inactivation no afterpotential D Drosophila melanogaster 4-8 11150331-5 2001 The INAD-TRP interaction is not required for targeting but rather for anchoring of complexes, because INAD and TRP can be targeted independently of each other. Tryptophan 9-12 inactivation no afterpotential D Drosophila melanogaster 102-106 11150331-5 2001 The INAD-TRP interaction is not required for targeting but rather for anchoring of complexes, because INAD and TRP can be targeted independently of each other. Tryptophan 111-114 inactivation no afterpotential D Drosophila melanogaster 4-8 10995445-6 2000 In addition, we demonstrated that TRP bound to INAD through the COOH terminus, and this interaction was required for localization of INAD. Tryptophan 34-37 inactivation no afterpotential D Drosophila melanogaster 47-51 10995445-6 2000 In addition, we demonstrated that TRP bound to INAD through the COOH terminus, and this interaction was required for localization of INAD. Tryptophan 34-37 inactivation no afterpotential D Drosophila melanogaster 133-137 10995445-10 2000 Rather, the primary function of the TRP/ INAD complex is to form the core unit required for localization of the signalplex to the rhabdomeres. Tryptophan 36-39 inactivation no afterpotential D Drosophila melanogaster 41-45 10766855-9 2000 Our findings indicate that INAD functions as RACK (receptor for activated PKC), allowing eye-PKC to phosphorylate INAD and TRP. Tryptophan 123-126 inactivation no afterpotential D Drosophila melanogaster 27-31