Proper function of the drosophila trp gene product during pupal development is important for normal visual transduction in the adult

Wong, Fulton; Schaefer, Edward J.; Roop, Barbara C.; Lamendola, Joseph; Johnson-Seaton, Diane; Shao, Dongguo

doi:10.1016/0896-6273(89)90117-7

Cited by 112 publications

(75 citation statements)

References 37 publications

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“…This sustained phase is absent in the trp mutant which was therefore proposed to be caused by a defect in the Ca 2+ influx pathway [6]. 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].…”

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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Section: ~ Introductionmentioning

confidence: 99%

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

et al. 1995

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“…Sequence motifs closely matching the RCS I consensus have been noted (Mismer and Rubin 1989; M. Fortini and C.S. Zuker, unpubl.I in the proximal 5' regions of several Drosophila genes expressed specifically in all or part of the photoreceptor cell population, namely trp (Montell and Rubin 1989;Wong et al 1989), ninaA (Schneuwly et al 1989;Shieh et al 1989), ninaC (Montell and Rubin 1988), chp , and arrestin (Smith et al 1990). RCS I may thus confer on a promoter the ability to be potentially activated in all photoreceptor cells, with more restricted cell-type specificities determined by upstream cis-acting elements.…”

Section: Report) D Virilis Rh3 and Rh4mentioning

confidence: 99%

Analysis of cis-acting requirements of the Rh3 and Rh4 genes reveals a bipartite organization to rhodopsin promoters in Drosophila melanogaster.

Fortini

Rubin²

1990

Genes Dev.

219

162

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The rhodopsin genes of Drosophila melanogaster are expressed in nonoverlapping subsets of photoreceptor cells within the insect visual system. Two of these genes, Rh3 and Rh4, are known to display complementary expression patterns in the UV-sensitive R7 photoreceptor cell population of the compound eye. In addition, we find that Rh3 is expressed in a small group of paired R7 and R8 photoreceptor cells at the dorsal eye margin that are apparently specialized for the detection of polarized light. In this paper we present a detailed characterization of the cis-acting requirements of both Rh3 and Rh4. Promoter deletion series demonstrate that small regulatory regions (<300 bp) of both R7 opsin genes contain DNA sequences sufficient to generate their respective expression patterns. Individual cis-acting elements were further identified by oligonucleotidedirected mutagenesis guided by interspecific sequence comparisons. Our results suggest that the Drosophila rhodopsin genes share a simple bipartite promoter structure, whereby the proximal region constitutes a functionally equivalent promoter "core" and the distal region determines cell-type specificity. The expression patterns of several hybrid rhodopsin promoters, in which all or part of the putative core regions have been replaced with the analogous regions of different rhodopsin promoters, provide additional evidence in support of this model.

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“…Journal of Endocrinology (2006) 191, 515-523 Introduction: response to osmotic stimuli -a function of TRPV ion channels, apparent since 'birth' of this subfamily Within the transient receptor potential (TRP) superfamily of ion channels (Cosens & Manning 1969, Montell & Rubin 1989, Wong et al 1989, Hardie & Minke 1992, Zhu et al 1995, the TRP vanilloid (TRPV) subfamily stepped into the spotlight in 1997 (Caterina et al 1997, Colbert et al 1997. The spectacular finding of the capsaicin receptor TRPV1 led to subsequent research in the direction of study of responses to ligand (capsaicin), acidity, and thermal stimuli.…”

Section: Introductionmentioning

confidence: 99%

Transient receptor potential vanilloid channels functioning in transduction of osmotic stimuli

Liedtke¹

2006

Journal of Endocrinology

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In signal transduction of metazoan cells, ion channels of the family of transient receptor potential (TRP) have been identified to respond to diverse external and internal stimuli, amongst them osmotic stimuli. This review will highlight findings on the TRPV subfamily, both vertebrate and invertebrate members. Out of the six mammalian TRP vanilloid (TRPV) channels, TRPV1, TRPV2, and TRPV4 were demonstrated to function in transduction of osmotic stimuli. TRPV channels have been found to function in cellular as well as systemic osmotic homeostasis in vertebrates. Invertebrate TRPV channels, five in Caenorhabditis elegans and two in Drosophila, have been shown to play a role in mechanosensation, such as hearing and proprioception in Drosophila and nose touch in C. elegans, and in the response to osmotic stimuli in C. elegans. In a striking example of evolutionary conservation of function, mammalian TRPV4 has been found to rescue osmoand mechanosensory deficits of the TRPV mutant strain osm-9 in C. elegans, despite not more than 26% orthology of the respective proteins.

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Proper function of the drosophila trp gene product during pupal development is important for normal visual transduction in the adult

Cited by 112 publications

References 37 publications

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

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

Analysis of cis-acting requirements of the Rh3 and Rh4 genes reveals a bipartite organization to rhodopsin promoters in Drosophila melanogaster.

Transient receptor potential vanilloid channels functioning in transduction of osmotic stimuli

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