Abnormal Electroretinogram from a Drosophila Mutant

Cosens, Derek; Manning, Aubrey

doi:10.1038/224285a0

Cited by 576 publications

(357 citation statements)

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“…6c) is the founding member of the TRP superfamily of cation channels [6,138], and mutation of trp results in a transient response to light (Fig. 3c) and a ∼10-fold decrease in Ca 2+ influx [8,139]. Disruption of trpl alone results in a decreased response to long light stimulation, but the phenotype is much more subtle than the transient response that is characteristic of trp flies [140].…”

Section: The Trpc Cation Channelsmentioning

confidence: 98%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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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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Section: The Trpc Cation Channelsmentioning

confidence: 98%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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“…The trp photoreceptors exhibit rapid decay of receptor potentials during a prolonged stimulus, thus named transient receptor potential (Fig. 1) (Cosens and Manning, 1969;Minke and Cook, 2002). However, double mutants of trp and trpl lacked complete light response of ion influx (Niemeyer et al, 1996;Reuss et al, 1997;Scott et al, 1997), showing that trp and trpl fulfill most of light-gated ion channels.…”

Section: Isolation Of Componentsmentioning

confidence: 99%

“…The trp fly, was first identified from a spontaneous mutant fly (Cosens and Manning, 1969) and later isolated from ERGbased screening (Pak and Leung, 2003). The trp photoreceptors exhibit rapid decay of receptor potentials during a prolonged stimulus, thus named transient receptor potential (Fig.…”

Section: Isolation Of Componentsmentioning

confidence: 99%

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Transient Receptor Potential Ion Channels and Animal Sensation: Lessons from Drosophila Functional Research

Kim¹

2004

BMB Reports

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Ion channels of the transient receptor potential (TRP) superfamily are non-selective cationic channels with six transmembrane domains. The TRP channel made its first debut as a light-gated Ca 2+ channel in Drosophila. Recently, research on animal sensation in Drosophila disclosed other members of the TRP family that are required for touch sensation and hearing as well as the sensation of painful stimuli.

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“…The first transient receptor potential (TRP) protein was discovered in studies that examined Drosophila phototransduction (1). The photoreceptor cells of Drosophila exhibit sustained receptor potentials in response to continuous light exposure.…”

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confidence: 99%

The Transient Receptor Potential Superfamily of Ion Channels

Huang

2004

Journal of the American Society of Nephrology

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Abstract. The transient receptor potential (TRP) superfamily of proteins is cation-selective ion channels with six predicted transmembrane segments and intracellularly localized amino and carboxyl termini. Members of the TRP superfamily are identified on the basis of amino acid sequence and structural similarity and are classified into TRPC, TRPV, TRPM, TRPP, TRPN, and TRPML subfamilies. TRP channels are widespread and have diverse functions, ranging from thermal, tactile, taste, osmolar, and fluid flow sensing to transepithelial Ca 2ϩ and Mg 2ϩ transport. Mutations of TRP proteins produce many renal diseases, including Mg 2ϩ wasting, hypocalcemia, and polycystic kidney diseases. This review focuses on recent advances in the understanding of their functions.The first transient receptor potential (TRP) protein was discovered in studies that examined Drosophila phototransduction (1). The photoreceptor cells of Drosophila exhibit sustained receptor potentials in response to continuous light exposure. The ionic basis for the sustained receptor potentials is influx of Ca 2ϩ from the extracellular space. Cosens and Manning (1) reported in 1969 that one group of mutant flies exhibits TRP upon continuous light exposure and named it trp, for transient receptor potential. The trp gene was cloned in 1989 (2) and subsequently shown to encode a Ca 2ϩ -permeable cation channel (3). Since then, many channels that bear sequence and structural similarities to the Drosophila TRP have been cloned from flies, worms, and mammals. Together, they form the TRP superfamily.Ion channels (e.g., voltage-gated K ϩ channels) are typically identified by their modes of activation and/or ion selectivity. Each family or superfamily of ion channels of similar activation and selectivity consists of multiple members of channel proteins with amino acid sequence homology. Unlike most ion channel families, the TRP superfamily of ion channels are identified on the basis of homology only. The mode of activation and selectivity for TRP channels are disparate. Some TRP channels are activated by ligands, whereas others are regulated by physical stimuli (e.g., heat) or yet-unknown mechanisms. All TRP channels are cation selective, but the selectivity ratio for Ca 2ϩ versus the monovalent cation Na ϩ (P Ca /P Na ) varies widely, ranging from Ͼ100:1, to 1 to 10:1, to Ͻ0.05:1. The lack of common identifying features has in part contributed to the confusing nomenclature of TRP channels in the literature.A recent consensus report proposed a unified nomenclature for the TRP superfamily (4). It classified TRP channels into TRPC, TRPV, and TRPM subfamilies. More recent classification has expanded TRP superfamily to include three additional, more distantly related subfamilies, TRPP, TRPML, and TRPN ( Figure 1). Structurally, all of these TRP channels have six predicted transmembrane (TM) segments and N-terminal and C-terminal cytoplasmic tails similar to topologies of voltagegated K ϩ , Na ϩ , and Ca 2ϩ channels; cyclic nucleotide-gated channels; and hyperpolarizati...

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Abnormal Electroretinogram from a Drosophila Mutant

Cited by 576 publications

References 6 publications

Phototransduction and retinal degeneration in Drosophila

Phototransduction and retinal degeneration in Drosophila

Transient Receptor Potential Ion Channels and Animal Sensation: Lessons from Drosophila Functional Research

The Transient Receptor Potential Superfamily of Ion Channels

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