Evidence map›Paper›PMID 10995445›Full record

ArticleThe Journal of cell biology2000

TRP and the PDZ protein, INAD, form the core complex required for retention of the signalplex in Drosophila photoreceptor cells.

H S Li, C Montell

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
  2. AnInsects · 2023
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  14. Drosophila visual transduction.Trends in neurosciences · 2012
    Review
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  19. Dependence on a retinophilin/myosin complex for stability of PKC and INAD and termination of phototransduction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

H S LiDepartment of Biological Chemistry and Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
C Montell
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

Unconventional roles for opsinsR01EY008117 · NEI · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI MONTELL, CRAIG · 1989 to 2022
$8.2M
TRP CHANNEL SIGNALING COMPLEX AND ITS ROLE IN VISIONR01EY010852 · NEI · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI MONTELL, CRAIG · 1995 to 2021
$7.9M
NEI NIH HHS EY08117NEI NIH HHS EY10852NEI NIH HHS R01 EY008117NEI NIH HHS R01 EY010852
6 · The paper itself

Abstract

The light response in Drosophila photoreceptor cells is mediated by a series of proteins that assemble into a macromolecular complex referred to as the signalplex. The central player in the signalplex is inactivation no afterpotential D (INAD), a protein consisting of a tandem array of five PDZ domains. At least seven proteins bind INAD, including the transient receptor potential (TRP) channel, which depends on INAD for localization to the phototransducing organelle, the rhabdomere. However, the determinants required for localization of INAD are not known. In this work, we showed that INAD was required for retention rather than targeting of TRP to the rhabdomeres. In addition, we demonstrated that TRP bound to INAD through the COOH terminus, and this interaction was required for localization of INAD. Other proteins that depend on INAD for localization, phospholipase C and protein kinase C, also mislocalized. However, elimination of any other member of the signalplex had no impact on the spatial distribution of INAD. A direct interaction between TRP and INAD did not appear to have a role in the photoresponse independent of localization of multiple signaling components. Rather, the primary function of the TRP/ INAD complex is to form the core unit required for localization of the signalplex to the rhabdomeres.

Indexed as

Drosophila ProteinsAge FactorsAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBinding SitesCalcium ChannelsDrosophilaElectrooculographyEye ProteinsMolecular Sequence DataMutagenesisPhotoreceptor Cells, InvertebrateProtein Kinase CProtein Structure, TertiarySynapsesCalcium ChannelsDrosophila ProteinsEye ProteinsinaD protein, DrosophilaProtein Kinase Ctransient receptor potential cation channel, subfamily C, member 1TRPC Cation ChannelsType C Phospholipases

Identifiers

PMID10995445
PMCPMC2150714
OpenAlexW1990140467

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.