Evidence map›Paper›PMID 21945483›Full record

ArticleVision research2011

Targeting of mouse guanylate cyclase 1 (Gucy2e) to Xenopus laevis rod outer segments.

Sukanya Karan, Beatrice M Tam, Orson L Moritz, Wolfgang Baehr

Open access · greenAbstract read
In one paragraph

Article in Vision research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Kinesin family 17 (osmotic avoidance abnormal-3) is dispensable for photoreceptor morphology and function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  2. Article
  3. Photoreceptors at a glance.Journal of cell science · 2015
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Protein sorting, targeting and trafficking in photoreceptor cells.Progress in retinal and eye research · 2013
    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 2 countries.

Sukanya KaranDepartment of Ophthalmology, John A. Moran Eye Center, University of Utah Health Science Center, Salt Lake City, UT 84132, USA.
Beatrice M Tam
Orson L Moritz
Wolfgang Baehr
University of British Columbia · CAUniversity of Utah · US

Funding

University of Utah, Core Vision Research GrantP30EY014800 · NEI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI PAUL STEVEN BERNSTEIN · 2005 to 2026
$14.6M
RETINAL PHOTORECEPTOR CYCLIC GMP PHOSPHODIESTERASER01EY008123 · NEI · UNIVERSITY OF UTAH · PI BAEHR, WOLFGANG · 1990 to 2019
$7.8M
Membrane Protein Transport in PhotoreceptorsR01EY019298 · NEI · UNIVERSITY OF UTAH · PI BAEHR, WOLFGANG · 2009 to 2018
$3.7M
CIHRNEI NIH HHS EY014800-039003NEI NIH HHS EY019298NEI NIH HHS EY08123NEI NIH HHS P30 EY014800NEI NIH HHS R01 EY008123NEI NIH HHS R01 EY019298
6 · The paper itself

Abstract

Photoreceptor guanylate cyclase (GC1) is a transmembrane protein and responsible for synthesis of cGMP, the secondary messenger of phototransduction. It consists of an extracellular domain, a single transmembrane domain, and an intracellular domain. It is unknown how GC1 targets to the outer segments where it resides. To identify a putative GC1 targeting signal, we generated a series of peripheral membrane and transmembrane constructs encoding extracellular and intracellular mouse GC1 fragments fused to EGFP. The constructs were expressed in Xenopus laevis rod photoreceptors under the control of the rhodopsin promoter. We examined the localization of GFP-GC1 fusion proteins containing the complete GC1 sequence, or partial GC1 sequences, which were membrane-associated via either the GC1 transmembrane domain or the rhodopsin C-terminal palmitoyl chains. Full-length GFP-GC1 targeted to the rod outer segment disk rims. As a group, fusion proteins containing the entire cytoplasmic domain of GC1 targeted to the OS, whereas other fusion proteins containing portions of the cytoplasmic or the extracellular domains did not. We conclude that GC1 likely has no single linear peptide-based OS targeting signal. Our results suggest targeting is due to either multiple weak signals in the cytoplasmic domain of GC1, or co-transport to the OS with an accessory protein.

Indexed as

AnimalsAnimals, Genetically ModifiedCell MembraneGuanylate CyclaseMembrane Fusion ProteinsMolecular Sequence DataProtein Sorting SignalsReceptors, Cell SurfaceRod Cell Outer SegmentXenopus laevisGuanylate CyclaseGucy2e protein, mouseMembrane Fusion ProteinsProtein Sorting SignalsReceptors, Cell Surface

Identifiers

PMID21945483
PMCPMC3205228
OpenAlexW2091790812

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.