Coexpression of
 Drosophila
 TRP and TRP-like proteins in
 Xenopus
 oocytes reconstitutes capacitative Ca
 2+
  entry

Gillo, Boaz; Chorna, Inna; Cohen, Hadas Achildiev; Cook, Boaz; Manistersky, I.; Chorev, Michael; Arnon, Assaf; Pollock, John A.; Selinger, Zvi; Minke, Barijch

doi:10.1073/pnas.93.24.14146

Cited by 97 publications

(71 citation statements)

References 53 publications

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“…One way to distinguish between Na + and Ca 2+ as mediators of the effect of TRPL on apoptosis would be to test the effect of expression of a Ca 2+ -selective member of the TRP family such as TRPV5, TRPV6 or possibly TRPC5 or TRPV1. 14 However, while heterologously expressed TRPL is often constitutively active, [15][16][17] it is less clear whether TRPV1, TRPV5, TRPV6, or TRPC5 are constitutively active.…”

Section: Discussionmentioning

confidence: 99%

“…This constitutive activity is thought to be due to differences between the environment of the Drosophila photoreceptor cell and the host animal cell, which lead to altered regulation of the opening of the TRPL channels. [15][16][17] The constitutive activity of TRPL causes a sustained increase in [Ca 2+ ] cyt , which can kill the transfected cells. [15][16][17] The aim of the present study was to express the Drosophila TRPL nonselective cation channel in a prostate cancer cell line and to test whether this leads to apoptosis and decreased cell survival.…”

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confidence: 99%

“…[15][16][17] The constitutive activity of TRPL causes a sustained increase in [Ca 2+ ] cyt , which can kill the transfected cells. [15][16][17] The aim of the present study was to express the Drosophila TRPL nonselective cation channel in a prostate cancer cell line and to test whether this leads to apoptosis and decreased cell survival. The experiments have been conducted using LNCaP cells, and a replication-deficient adenovirus to deliver TRPL cDNA into LNCaP cells.…”

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Expression of Drosophila Ca2+ permeable transient receptor potential-like channel protein in a prostate cancer cell line decreases cell survival

et al. 2003

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The effects of expression of Drosophila melanoga ster Ca 2+ permeable transient receptor potential-like (TRPL) channels, under the control of the cytomegalovirus (CMV) or prostate cell-specific promoters, on cell survival and apoptosis in the androgen-sensitive LNCaP prostate cancer cell line were investigated. A prostate-specific antigen (PSA) promoter construct (designated PSAEn/PSAPr) composed of a 0.6 kb region of the promoter and a 1.45 kb region of the enhancer resulted in androgen-dependent and prostatespecific expression of a luciferase reporter gene in transiently transfected LNCaP cells. Expression of the enhanced green fluorescence protein-TRPL chimeric protein under the control of the CMV promoter was confirmed by Western blot. Whereas the majority of the expressed protein was located in the cytoplasmic space, confocal microscopy with the CD-9 protein as a plasma membrane marker demonstrated that approximately 10% of the expressed TRPL protein was located in a band in the plasma membrane. Using recombinant adenoviruses, expression of the TRPL protein was associated with an increase in both the initial and sustained rates of Ca 2+ inflow. Expression of TRPL under the control of the CMV promoter for 96 hours decreased cell number and increased the number of cells undergoing apoptosis by 23 and 27%, respectively. Apoptosis was inhibited by a caspase-3 inhibitor, Z-DEVD-fmk. It is concluded that, when heterologously expressed in LNCaP cells, the TRPL protein leads to a reduction in cell survival due, in part, to the induction of apoptosis. The effects of TRPL are likely caused by enhanced Na + and Ca 2+ inflow to the cells. This finding suggests a novel approach to modify the growth of prostate cancer cells that fail to undergo apoptosis following androgen ablation therapy.

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Expression of Drosophila Ca2+ permeable transient receptor potential-like channel protein in a prostate cancer cell line decreases cell survival

et al. 2003

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“…Functional TRP channels are supposed to result following the assembly of four TRP subunits. Although multimerization has been already demonstrated for various members of the TRP family (including TRPV4) (21)(22)(23)(24)(25), the tetrameric structure has only been proposed for a few TRP channels (26 -28).…”

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Human TRPV4 Channel Splice Variants Revealed a Key Role of Ankyrin Domains in Multimerization and Trafficking

Arniges

Fernández-Fernández

Albrecht

et al. 2006

Journal of Biological Chemistry

166

150

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The TRPV4 cation channel exhibits a topology consisting of six predicted transmembrane domains (TM) with a putative pore loop between TM5 and TM6 and intracellular N-and C-tails, the former containing at least three ankyrin domains. Functional transient receptor potential (TRP) channels are supposed to result following the assembly of four subunits. However, the rules governing subunit assembly and protein domains implied in this process are only starting to emerge. The ankyrin, TM, and the C-tail domains have been identified as important determinants of the oligomerization process. We now describe the maturation and oligomerization of five splice variants of the TRPV4 channel. The already known TRPV4-A and TRPV4-B (⌬384 -444) variants and the new TRPV4-C (⌬237-284), TRPV4-D (⌬27-61), and TRPV4-E (⌬237-284 and ⌬384 -444) variants. All alternative spliced variants involved deletions in the cytoplasmic N-terminal region, affecting (except for TRPV4-D) the ankyrin domains. Subcellular localization, fluorescence resonance energy transfer, co-immunoprecipitation, glycosylation profile, and functional analysis of these variants permitted us to group them into two classes: group I (TRPV4-A and TRPV4-D) and group II (TRPV4-B, TRPV4-C, and TRPV4-E). Group I, unlike group II variants, were correctly processed, homo-and heteromultimerized in the endoplasmic reticulum, and were targeted to the plasma membrane where they responded to typical TRPV4 stimuli. Our results suggest that: 1) TRPV4 biogenesis involves core glycosylation and oligomerization in the endoplasmic reticulum followed by transfer to the Golgi apparatus for subsequent maturation; 2) ankyrin domains are necessary for oligomerization of TRPV4; and 3) lack of TRPV4 oligomerization determines its accumulation in the endoplasmic reticulum.The non-selective cation channel TRPV4 is a member of the transient receptor potential (TRP) 3 family of channels (1). TRPV4 shows multiple modes of activation and regulatory sites, enabling it to respond to various stimuli, including osmotic cell swelling (2-5), mechanical stress (6 -8), heat (9), acidic pH (7), endogenous ligands (10), high viscous solutions (11), and synthetic agonists such as 4␣-phorbol 12,13-didecanoate (4␣-PDD) (12). TRPV4 mRNA is expressed in a broad range of tissues (13), although functional tests have only been carried out in a few: endothelial (14), epithelial (5,11,15), smooth muscle (16), keratinocytes (17), and DRG neurons (18). An alternative splice variant lacking the seventh exon has also been cloned from human aortic endothelial cells (19), although this variant was not further investigated because of its unresponsiveness to hypotonic stimuli.The general topology of a TRP subunit consists of six predicted transmembrane domains (TM) with a putative pore loop between TM5 and TM6 and intracellular N-and C-terminal regions of variable length, the former containing multiple ankyrin (ANK) repeats in the TRPC, TRPA, TRPN, and TRPV subfamilies (1). ANK repeats are modular protein interaction domains, ...

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“…Although the reduction in the amount of the TRP protein may contribute to these phenotypes, several lines of evidence support the view that inaF mutations also more directly affect the TRP channel function, suggesting that the INAF protein may have a regulatory role in the channel function. P hototransduction in Drosophila utilizes a phospholipase C (PLC)-mediated signaling cascade (1-3) and activates two classes of light-sensitive channels (4)(5)(6)(7)(8), a Ca 2ϩ -selective class and a nonselective cation class. A growing body of evidence suggests that the Ca 2ϩ -selective channels are formed by the protein product of the trp gene (5,9).…”

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INAF, a protein required for transient receptor potential Ca ²⁺ channel function

Geng

Leung

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

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The trp gene of Drosophila encodes a subunit of a class of Ca 2؉ -selective light-activated channels that carry the bulk of the phototransduction current. Transient receptor potential (TRP) homologs have been identified throughout animal phylogeny. In vertebrates, TRP-related channels have been suggested to mediate ''store-operated Ca 2؉ entry,'' which is important in Ca 2؉ homeostasis in a wide variety of cell types. However, the mechanisms of activation and regulation of the TRP channel are not known. Here, we report on the Drosophila inaF gene, which encodes a highly eye-enriched protein, INAF, that appears to be required for TRP channel function. A null mutation in this gene significantly reduces the amount of the TRP protein and, in addition, specifically affects the TRP channel function so as to nearly shut down its activity. The inaF mutation also dramatically suppresses the severe degeneration caused by a constitutively active mutation in the trp gene. Although the reduction in the amount of the TRP protein may contribute to these phenotypes, several lines of evidence support the view that inaF mutations also more directly affect the TRP channel function, suggesting that the INAF protein may have a regulatory role in the channel function.

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Coexpression of Drosophila TRP and TRP-like proteins in Xenopus oocytes reconstitutes capacitative Ca ²⁺ entry

Cited by 97 publications

References 53 publications

Expression of Drosophila Ca2+ permeable transient receptor potential-like channel protein in a prostate cancer cell line decreases cell survival

Expression of Drosophila Ca2+ permeable transient receptor potential-like channel protein in a prostate cancer cell line decreases cell survival

Human TRPV4 Channel Splice Variants Revealed a Key Role of Ankyrin Domains in Multimerization and Trafficking

INAF, a protein required for transient receptor potential Ca ²⁺ channel function

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Coexpression of Drosophila TRP and TRP-like proteins in Xenopus oocytes reconstitutes capacitative Ca 2+ entry

Cited by 97 publications

References 53 publications

Expression of Drosophila Ca2+ permeable transient receptor potential-like channel protein in a prostate cancer cell line decreases cell survival

Expression of Drosophila Ca2+ permeable transient receptor potential-like channel protein in a prostate cancer cell line decreases cell survival

Human TRPV4 Channel Splice Variants Revealed a Key Role of Ankyrin Domains in Multimerization and Trafficking

INAF, a protein required for transient receptor potential Ca 2+ channel function

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Coexpression of Drosophila TRP and TRP-like proteins in Xenopus oocytes reconstitutes capacitative Ca ²⁺ entry

INAF, a protein required for transient receptor potential Ca ²⁺ channel function