Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene

Phillips, A. Marie; Bull, Ann; Kelly, Luke T.

doi:10.1016/0896-6273(92)90085-r

Cited by 413 publications

(339 citation statements)

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“…These include the demonstration that the cascade operates through activation of a phospholipase Cβ (PLC) [5] and opening of the TRP and TRPL cation channels [6][7][8][9] (Fig. 1).…”

Section: Overview and Relationship Of Drosophila To Mammalian Phototrmentioning

confidence: 99%

“…4), and modulation of the cation influx channels. Both TRP [173] and TRPL [7,174] bind CaM through C-terminal sequences in vitro. In the absence of TRP, expression of a TRPL isoform missing either of two CaM binding sites leads to remarkably slower termination than that observed in photoreceptors expressing wild-type TRPL only [159].…”

Section: Ca 2+ -Dependent Termination Of the Photoresponsementioning

confidence: 99%

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Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

255

300

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Drosophila visual transduction is the fastest known G-protein-coupled signaling cascade and has therefore served as a genetically tractable animal model for characterizing rapid responses to sensory stimulation. Mutations in over 30 genes have been identified, which affect activation, adaptation, or termination of the photoresponse. Based on analyses of these genes, a model for phototransduction has emerged, which involves phosphoinoside signaling and culminates with opening of the TRP and TRPL cation channels. Many of the proteins that function in phototransduction are coupled to the PDZ containing scaffold protein INAD and form a supramolecular signaling complex, the signalplex. Arrestin, TRPL, and Gα q undergo dynamic light-dependent trafficking, and these movements function in long-term adaptation. Other proteins play important roles either in the formation or maturation of rhodopsin, or in regeneration of phosphatidylinositol 4,5-bisphosphate (PIP 2 ), which is required for the photoresponse. Mutation of nearly any gene that functions in the photoresponse results in retinal degeneration. The underlying bases of photoreceptor cell death are diverse and involve mechanisms such as excessive endocytosis of rhodopsin due to stable rhodopsin/arrestin complexes and abnormally low or high levels of Ca 2+ . Drosophila visual transduction appears to have particular relevance to the cascade in the intrinsically photosensitive retinal ganglion cells in mammals, as the photoresponse in these latter cells appears to operate through a remarkably similar mechanism.

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“…These include the demonstration that the cascade operates through activation of a phospholipase Cβ (PLC) [5] and opening of the TRP and TRPL cation channels [6][7][8][9] (Fig. 1).…”

Section: Overview and Relationship Of Drosophila To Mammalian Phototrmentioning

confidence: 99%

Section: Ca 2+ -Dependent Termination Of the Photoresponsementioning

confidence: 99%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

255

300

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“…Candidates involved in voltage-independent Ca 2+ entry into [9]. A detailed analysis of the trpl sequence showed that it shares moderate homology with voltage-dependent Ca 2+ and Na ÷ channels at their putative transmembrane regions.…”

Section: ~ Introductionmentioning

confidence: 99%

“…The trp gene was cloned [7,8]. Subsequently, molecular cloning of a Drosophila calmodulin binding protein showed it to be a homologue of the trp gene product and named trp-like or trpl [9]. A detailed analysis of the trpl sequence showed that it shares moderate homology with voltage-dependent Ca 2+ and Na ÷ channels at their putative transmembrane regions.…”

Section: ~ Introductionmentioning

confidence: 99%

Molecular cloning of a widely expressed human homologue for the Drosophila trp gene

et al. 1995

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The Drosophila transient receptor potential (trp) gene and its homologue, trpl, have been suggested to mediate calcium entry during the insect's phototransduction process. We isolated human cDNA, human trp-1 (Htrp-1), encoding a polypeptide .f 793 amino acids that is 37% identical (62% similar) to Drosophila trp and trpl. Northern analysis showed that the Htrp-1 transcript is approximately 5.5 kb and expressed in most human tissues, with higher amounts in ovary, testis, heart, and brain.Isolation of Htrp-I suggests that a trp-type protein is present in mammals and should provide a useful tool in studying calciumdepletion induced calcium influx processes.:~ey words': Transient receptor potential; Calcium influx , hannel; Ca 2+ signaling ~. IntroductionCalcium regulation plays an important role in many cellular 0rocesses. In non-excitable mammalian cells, activation of i~hosphoinositide-specific phospholipase C (PLC) produces ~nositol 1,4,5-trisphosphate (IP3), which in turn causes the reease of intracellular calcium from its storage pools in the endo~lasmic reticulum. This results in a transient elevation of cyosolic-free Ca 2+, which is normally followed by a Ca 2+ influx 'rom the extracellular space. By refilling the pools, Ca 2+ influx )lays an important role in prolonging the Ca 2+ signal, allowing or localized signaling, and maintaining Ca 2÷ oscillations [1].Calcium influx in non-excitable cells is thought to occur hrough plasma membrane channels which, in contrast to the voltage-dependent Ca 2+ channels in excitable cells, are operated lot by changes of membrane potentials but rather by how full he internal Ca 2+ stores are [2]. Although studies using either luorescent Ca 2+ indicators or electrophysiological techniques lave suggested that multiple types of Ca 2+ permeant channels nay be involved in different cell types to fulfill the influx funcion, the molecular structure of the channels and the mechalism that regulates the influx have remained unclear and reprerent one of the major unanswered questions of cellular Ca -,+ !lomeostasis [3][4][5].Candidates involved in voltage-independent Ca 2+ entry into [9]. A detailed analysis of the trpl sequence showed that it shares moderate homology with voltage-dependent Ca 2+ and Na ÷ channels at their putative transmembrane regions. However, in clear contrast with the voltage-dependent channels, it lacks the positively charged amino acid residues at the presumed $4 segment which are thought to act as voltage sensors that promote gating in response to changes in membrane potentials. The structural homology to Ca 2+ and Na + channels together with the absence of charged residues in trpl and trp suggested that these proteins may form voltage-independent ion channels. This was demonstrated recently by expression of the cDNAs for trp and trpl in insect Sf9 cells using the baculovirus system. It was fount that trp forms a Ca 2÷ permeable cation channel which is activated by store depletion with thapsigargin [10] whereas trpl forms a Ca -'+ permeable non-selec...

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“…Binding and regulation of TRP channels via calmodulin (CAM) appears to be a rather common modulatory mechanism that has already been described for the founding members of the family, the Drosophila TRP and TRPL channels (Phillips et al 1992;Warr and Kelly 1996;Scott et al 1997). Here, we will concentrate on the regulation of TRPV channels by calmodulin.…”

Section: Regulation By Calmodulinmentioning

confidence: 97%

Structure-function analysis of TRPV channels

Niemeyer

2005

Naunyn-Schmiedeberg's Arch Pharmacol

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In recent years many new members of the family of TRP ion channels have been identified. These channels are classified into several subgroups and participate in many sensory and physiological functions. TRPV channels are important for the perception of pain, temperature sensing, osmotic regulation, and maintenance of calcium homeostasis, and much recent research concerns the identification of protein domains involved in mediating specific channel functions. Recent literature on TRPV channel subunit composition, protein domains required for subunit assembly, trafficking, and regulation will be reviewed and discussed.

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Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene

Cited by 413 publications

References 59 publications

Phototransduction and retinal degeneration in Drosophila

Phototransduction and retinal degeneration in Drosophila

Molecular cloning of a widely expressed human homologue for the Drosophila trp gene

Structure-function analysis of TRPV channels

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