Evidence map›Paper›PMID 23672200›Full record

ArticleJournal of proteome research2013

Proteomic identification of unique photoreceptor disc components reveals the presence of PRCD, a protein linked to retinal degeneration.

Nikolai P Skiba, William J Spencer, Raquel Y Salinas, Eric C Lieu, J Will Thompson, Vadim Y Arshavsky

Abstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

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  9. The WAVE complex drives the morphogenesis of the photoreceptor outer segment cilium.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  17. Photoreceptor Discs: Built Like Ectosomes.Trends in cell biology · 2020
    Review
  18. Article
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Nikolai P SkibaAlbert Eye Research Institute, 2Institute for Genome Sciences & Policy, Duke University School of Medicine, Durham, North Carolina 27710, United States.
William J Spencer
Raquel Y Salinas
Eric C Lieu
J Will Thompson
Vadim Y Arshavsky
Smith-Kettlewell Eye Research Institute · USDuke University · US

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
ORGANIZATION AND FUNCTIONS OF CELLULAR STRUCTUREST32GM007184 · NIGMS · DUKE UNIVERSITY · PI JINKS-ROBERTSON, SUE · 1985 to 2019
$18.2M
Molecular mechanisms of photoreceptor outer segment morphogenesisR01EY012859 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI ARSHAVSKY, VADIM Y · 2000 to 2022
$10.0M
NEI NIH HHS EY12859NEI NIH HHS EY5722NEI NIH HHS P30 EY005722NEI NIH HHS R01 EY012859NIGMS NIH HHS T32 GM007184
6 · The paper itself

Abstract

Visual signal transduction takes place on the surface of flat membrane vesicles called photoreceptor discs, which reside inside the light-sensitive outer segment organelle of vertebrate photoreceptor cells. Although biochemical studies have indicated that discs are built with a handful of highly specialized proteins, proteomic studies have yielded databases consisting of hundreds of entries. We addressed this controversy by employing protein correlation profiling, which allows identification of unique components of organelles that can be fractionated but not purified to absolute homogeneity. We subjected discs to sequential steps of fractionation and identified the relative amounts of proteins in each fraction by label-free quantitative mass spectrometry. This analysis demonstrated that the photoreceptor disc proteome contains only eleven components, which satisfy the hallmark criterion for being unique disc-resident components: the retention of a constant molar ratio among themselves across fractionation steps. Remarkably, one of them is PRCD, a protein whose mutations have been shown to cause blindness, yet cellular localization remained completely unknown. Identification of PRCD as a novel disc-specific protein facilitates understanding its functional role and the pathobiological significance of its mutations. Our study provides a striking example how protein correlation profiling allows a distinction between constitutive components of cellular organelles and their inevitable contaminants.

Indexed as

Amino Acid SequenceAnimalsCattleCell FractionationEye ProteinsGene ExpressionGene Expression ProfilingHumansMass SpectrometryMolecular Sequence DataMutationProteomicsRetinal DegenerationRetinal Photoreceptor Cell Outer SegmentEye ProteinsPRCD protein, human

Identifiers

PMID23672200
PMCPMC3771658
OpenAlexW2061017540

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.