Evidence map›Paper›PMID 9679151›Full record

ArticleThe Journal of cell biology1998

Coordination of an array of signaling proteins through homo- and heteromeric interactions between PDZ domains and target proteins.

X Z Xu, A Choudhury, X Li, C Montell

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
8.1field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 213 citations in OpenAlex.

  1. Homer condensates orchestrate YAP-Wnt signaling crosstalk downstream of the Crumbs polarity complex.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. AnInsects · 2023
    Article
  4. Review
  5. Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019
    Review
  6. Calmodulin Enhances Cryptochrome Binding to INAD inFrontiers in molecular neuroscience · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Syntrophin proteins as Santa Claus: role(s) in cell signal transduction.Cellular and molecular life sciences : CMLS · 2013
    Review
  13. Article
  14. Review
  15. Drosophila visual transduction.Trends in neurosciences · 2012
    Review
  16. Review
  17. Article
  18. The history of TRP channels, a commentary and reflection.Pflugers Archiv : European journal of physiology · 2011
    Review
  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. CFTR chloride channel in the apical compartments: spatiotemporal coupling to its interacting partners.Integrative biology : quantitative biosciences from nano to macro · 2010
    Review
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

4 authors at 2 institutions in 1 country.

X Z XuDepartment of Biological Chemistry and Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
A Choudhury
X Li
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
NEI NIH HHS EY08117NEI NIH HHS R01 EY008117
6 · The paper itself

Abstract

The rapid activation and feedback regulation of many G protein signaling cascades raises the possibility that the critical signaling proteins may be tightly coupled. Previous studies show that the PDZ domain containing protein INAD, which functions in Drosophila vision, coordinates a signaling complex by binding directly to the light-sensitive ion channel, TRP, and to phospholipase C (PLC). The INAD signaling complex also includes rhodopsin, protein kinase C (PKC), and calmodulin, though it is not known whether these proteins bind to INAD. In the current work, we show that rhodopsin, calmodulin, and PKC associate with the signaling complex by direct binding to INAD. We also found that a second ion channel, TRPL, bound to INAD. Thus, most of the proteins involved directly in phototransduction appear to bind to INAD. Furthermore, we found that INAD formed homopolymers and the homomultimerization occurred through two PDZ domains. Thus, we propose that the INAD supramolecular complex is a higher order signaling web consisting of an extended network of INAD molecules through which a G protein-coupled cascade is tethered.

Indexed as

Drosophila ProteinsAnimalsBinding SitesCalmodulinCalmodulin-Binding ProteinsDrosophilaEye ProteinsInsect ProteinsIon ChannelsMacromolecular SubstancesMembrane ProteinsMutagenesis, Site-DirectedPhotoreceptor Cells, InvertebrateProtein BindingProtein Kinase CRhodopsinCalmodulinCalmodulin-Binding Proteinscno protein, DrosophilaDrosophila ProteinsEye ProteinsinaD protein, DrosophilaInsect ProteinsIon ChannelsMacromolecular SubstancesMembrane ProteinsProtein Kinase CRhodopsinRod OpsinsTransient Receptor Potential Channelstrpl protein, Drosophila

Identifiers

PMID9679151
PMCPMC2133053
OpenAlexW2170170370

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.