Evidence map›Paper›PMID 16524428›Full record

ArticlePigment cell research2006

The melanosomal/lysosomal protein OA1 has properties of a G protein-coupled receptor.

Giulio Innamorati, Rosanna Piccirillo, Paola Bagnato, Ilaria Palmisano, Maria Vittoria Schiaffino

Open access · greenAbstract read
In one paragraph

Article in Pigment cell research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.2field-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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. CRISPR-AsCas12a Efficiently Corrects aThe CRISPR journal · 2022
    Article
  4. Review
  5. Melanosome Biogenesis in the Pigmentation of Mammalian Skin.Integrative and comparative biology · 2021
    Review
  6. Article
  7. Bioinformatics analysis of key biomarkers for retinoblastoma.The Journal of international medical research · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Ocular Albinism Type 1 Regulates Melanogenesis in Mouse Melanocytes.International journal of molecular sciences · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Ion transport in pigmentation.Archives of biochemistry and biophysics · 2014
    Review
  17. GPCR signaling along the endocytic pathway.Current opinion in cell biology · 2014
    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

5 authors at 1 institution in 1 country.

Giulio InnamoratiDIBIT, Scientific Institute San Raffalele, Via Olgettina 58, 20132 Milan, Italy.
Rosanna Piccirillo
Paola Bagnato
Ilaria Palmisano
Maria Vittoria Schiaffino
San Raffaele University of Rome · IT

Funding

Dissecting the Molecular Basis of Ocular Albinism type 1R01EY014540 · NEI · FONDAZONE CENT/SAN RAFFAELE/DEL MONTE · PI SCHIAFFINO, MARIA VITTORIA · 2003 to 2007
$935k
NEI NIH HHS 5R01EY014540NEI NIH HHS R01 EY014540Telethon F.3
6 · The paper itself

Abstract

The protein product of the ocular albinism type 1 gene, named OA1, is a pigment cell-specific integral membrane glycoprotein, localized to melanosomes and lysosomes and possibly implicated in melanosome biogenesis. Although its function remains unknown, we previously showed that OA1 shares structural similarities with G protein-coupled receptors (GPCRs). To ascertain the molecular function of OA1 and in particular its nature as a GPCR, we adopted a heterologous expression strategy commonly exploited to demonstrate GPCR-mediated signaling in mammalian cells. Here we show that when expressed in COS7 cells OA1 displays a considerable and spontaneous capacity to activate heterotrimeric G proteins and the associated signaling cascade. In contrast, OA1 mutants carrying either a missense mutation or a small deletion in the third cytosolic loop lack this ability. Furthermore, OA1 is phosphorylated and interacts with arrestins, well-established multifunctional adaptors of conformationally active GPCRs. In fact, OA1 colocalizes and coprecipitates with arrestins, which downregulate the signaling of OA1 by specifically reducing its expression levels. These findings indicate that heterologously expressed OA1 exhibits two fundamental properties of GPCRs, being capable to activate heterotrimeric G proteins and to functionally associate with arrestins, and provide proof of principle that OA1 can actually function as a canonical GPCR in mammalian cells.

Indexed as

Amino Acid SequenceAnimalsArrestinsChlorocebus aethiopsCOS CellsEye ProteinsGene ExpressionGTP-Binding ProteinsHumansLysosomesMelanosomesMembrane GlycoproteinsProtein BindingProtein Processing, Post-TranslationalReceptors, G-Protein-CoupledSequence DeletionArrestinsEye ProteinsGPR143 protein, humanGTP-Binding ProteinsMembrane GlycoproteinsReceptors, G-Protein-Coupled

Identifiers

PMID16524428
PMCPMC1459912
OpenAlexW2059735420

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.