Evidence map›Paper›PMID 26420485›Full record

ArticleThe Journal of biological chemistry2015

Retinal Degeneration Slow (RDS) Glycosylation Plays a Role in Cone Function and in the Regulation of RDS·ROM-1 Protein Complex Formation.

Michael W Stuck, Shannon M Conley, Muna I Naash

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Glycosylation of the retina.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Novel molecular mechanisms for Prph2-associated pattern dystrophy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Tetraspanins Function as Regulators of Cellular Signaling.Frontiers in cell and developmental biology · 2017
    Review
  16. Article
  17. 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

3 authors at 1 institution in 1 country.

Michael W StuckFrom the Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104.
Shannon M ConleyFrom the Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104.
Muna I NaashFrom the Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104 mnaash@central.uh.edu.
University of Oklahoma Health Sciences Center · US

Funding

Translational Core for Therapeutic and Diagnostic DevelopmentP30EY001792 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI AAKALU, VINAY · 1985 to 2025
$14.8M
Supplement for: Mechanism of Photoreceptor Cell Degeneration in Animal Models of Retinal DiseasesR01EY010609 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI MUAYYAD R AL-UBAIDI, Muna I. Naash · 1995 to 2026
$11.0M
Vision Science Training ProgramT32EY023202 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI CALLEGAN, MICHELLE C · 2014 to 2025
$952k
NEI NIH HHS P30 EY001792NEI NIH HHS R01 EY010609NEI NIH HHS R01EY010609NEI NIH HHS T32 EY023202NEI NIH HHS T32EY023202
6 · The paper itself

Abstract

The photoreceptor-specific glycoprotein retinal degeneration slow (RDS, also called PRPH2) is necessary for the formation of rod and cone outer segments. Mutations in RDS cause rod and cone-dominant retinal disease, and it is well established that both cell types have different requirements for RDS. However, the molecular mechanisms for this difference remain unclear. Although RDS glycosylation is highly conserved, previous studies have revealed no apparent function for the glycan in rods. In light of the highly conserved nature of RDS glycosylation, we hypothesized that it is important for RDS function in cones and could underlie part of the differential requirement for RDS in the two photoreceptor subtypes. We generated a knockin mouse expressing RDS without the N-glycosylation site (N229S). Normal levels of RDS and the unglycosylated RDS binding partner rod outer segment membrane protein 1 (ROM-1) were found in N229S retinas. However, cone electroretinogram responses were decreased by 40% at 6 months of age. Because cones make up only 3-5% of photoreceptors in the wild-type background, N229S mice were crossed into the nrl(-/-) background (in which all rods are converted to cone-like cells) for biochemical analysis. In N229S/nrl(-/-) retinas, RDS and ROM-1 levels were decreased by ~60% each. These data suggest that glycosylation of RDS is required for RDS function or stability in cones, a difference that may be due to extracellular versus intradiscal localization of the RDS glycan in cones versus rods.

Indexed as

Protein Processing, Post-TranslationalAnimalsEye ProteinsGene Knock-In TechniquesGlycosylationMembrane ProteinsMiceMice, Mutant StrainsMultiprotein ComplexesMutationPeripherinsProtein MultimerizationRetinal Cone Photoreceptor CellsRetinal Rod Photoreceptor CellsTetraspaninsEye ProteinsMembrane ProteinsMultiprotein ComplexesPeripherinsPrph2 protein, mouseRom1 protein, mouseTetraspaninsglycosylationN229Soligomerizationperipherin-2photoreceptorretinatetraspanin

Identifiers

PMID26420485
PMCPMC4646032
OpenAlexW2263962702

What OpenQuestion holds

Textmetadata
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.