Evidence map›Paper›PMID 26456832›Full record

ArticleCell reports2015

TRP and Rhodopsin Transport Depends on Dual XPORT ER Chaperones Encoded by an Operon.

Zijing Chen, Hsiang-Chin Chen, Craig Montell

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. A day sleep promoting role of phototransduction inNeurobiology of sleep and circadian rhythms · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Rapid Release of CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  8. 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

3 authors at 1 institution in 1 country.

Zijing ChenNeuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106, USA; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA 93106, USA.
Hsiang-Chin ChenNeuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106, USA; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA 93106, USA.
Craig MontellNeuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106, USA; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA 93106, USA. Electronic address: craig.montell@lifesci.ucsb.edu.
University of California, Santa Barbara · 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 EY008117NEI NIH HHS EY010852NEI NIH HHS R01 EY008117NEI NIH HHS R01 EY010852
6 · The paper itself

Abstract

TRP channels and G protein-coupled receptors (GPCRs) play critical roles in sensory reception. However, the identities of the chaperones that assist GPCRs in translocating from the endoplasmic reticulum (ER) are limited, and TRP ER chaperones are virtually unknown. The one exception for TRPs is Drosophila XPORT. Here, we show that the xport locus is bicistronic and encodes unrelated transmembrane proteins, which enable the signaling proteins that initiate and culminate phototransduction, rhodopsin 1 (Rh1) and TRP, to traffic to the plasma membrane. XPORT-A and XPORT-B are ER proteins, and loss of either has a profound impact on TRP and Rh1 targeting to the light-sensing compartment of photoreceptor cells. XPORT-B complexed in vivo with the Drosophila homolog of the mammalian HSP70 protein, GRP78/BiP, which, in turn, associated with Rh1. Our work highlights a coordinated network of chaperones required for the biosynthesis of the TRP channel and rhodopsin in Drosophila photoreceptor cells.

Indexed as

OperonAnimalsDrosophilaDrosophila ProteinsEndoplasmic ReticulumHSP70 Heat-Shock ProteinsMolecular ChaperonesProtein BindingProtein TransportRhodopsinTransient Receptor Potential ChannelsDrosophila ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesRhodopsinTransient Receptor Potential ChannelsXport-A protein, Drosophila

Identifiers

PMID26456832
PMCPMC4618092
OpenAlexW1898962888

What OpenQuestion holds

Textmetadata
LicenceTDM
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.