Evidence map›Paper›PMID 22099462›Full record

ArticleNeuron2011

XPORT-dependent transport of TRP and rhodopsin.

Erica E Rosenbaum, Kimberley S Brehm, Eva Vasiljevic, Che-Hsiung Liu, Roger C Hardie, Nansi Jo Colley

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Neuron, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Cnpy1 is a candidate endoplasmic reticulum chaperone of vomeronasal type 2 GPCRs.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Knockdown of Dehydrodolichyl Diphosphate Synthase in theFrontiers in molecular neuroscience · 2021
    Article
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  10. Review
  11. Article
  12. TRPV1 channels and the progesterone receptor Sig-1R interact to regulate pain.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Organization of theeLife · 2017
    Article
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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

6 authors at 3 institutions in 2 countries.

Erica E RosenbaumDepartment of Ophthalmology and Visual Sciences, Department of Genetics, and Eye Research Institute, University of Wisconsin, Madison, WI 53792, USA.
Kimberley S Brehm
Eva Vasiljevic
Che-Hsiung Liu
Roger C Hardie
Nansi Jo Colley
Smith-Kettlewell Eye Research Institute · USUniversity of Cambridge · GBUniversity of Wisconsin–Madison · US

Funding

UW Vision Research Core - Administrative CoreP30EY016665 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERT W NICKELLS · 2005 to 2026
$12.6M
NEUROSCIENCE TRAINING PROGRAMT32GM007507 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HALLORAN, MARY C · 1985 to 2017
$9.3M
MOLECULAR STUDIES OF RETINAL DEGENERATION IN DROSOPHILAR01EY008768 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI COLLEY, NANSI J. · 1995 to 2016
$5.3M
MOLECULAR STUDIES OF RETINAL DEGENERATION IN DROSOPHILAR29EY008768 · NEI · UNIVERSITY OF WISCONSIN MADISON · PI COLLEY, NANSI J. · 1990 to 1994
–
Biotechnology and Biological Sciences Research Council BB/G006865/1NEI NIH HHS EY008768NEI NIH HHS P30 EY016665NEI NIH HHS R01 EY008768NIA NIH HHS AG321762NIGMS NIH HHS T32 GM007507NIGMS NIH HHS T32GM007507
6 · The paper itself

Abstract

TRP channels have emerged as key biological sensors in vision, taste, olfaction, hearing, and touch. Despite their importance, virtually nothing is known about the folding and transport of TRP channels during biosynthesis. Here, we identify XPORT (exit protein of rhodopsin and TRP) as a critical chaperone for TRP and its G protein-coupled receptor (GPCR), rhodopsin (Rh1). XPORT is a resident ER and secretory pathway protein that interacts with TRP and Rh1, as well as with Hsp27 and Hsp90. XPORT promotes the targeting of TRP to the membrane in Drosophila S2 cells, a finding that provides a critical first step toward solving a longstanding problem in the successful heterologous expression of TRP. Mutations in xport result in defective transport of TRP and Rh1, leading to retinal degeneration. Our results identify XPORT as a molecular chaperone and provide a mechanistic link between TRP channels and their GPCRs during biosynthesis and transport.

Indexed as

AnimalsCell LineDrosophilaDrosophila ProteinsMolecular ChaperonesPhotoreceptor Cells, InvertebrateProtein TransportRhodopsinTRPC Cation ChannelsDrosophila ProteinsMolecular ChaperonesRhodopsinTRPC Cation ChannelsXport-A protein, Drosophila

Identifiers

PMID22099462
PMCPMC3234208
OpenAlexW2040323799

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.