Evidence map›Paper›PMID 22570474›Full record

ArticleThe Journal of biological chemistry2012

Receptor-transporting protein 1 short (RTP1S) mediates translocation and activation of odorant receptors by acting through multiple steps.

Lifang Wu, Yi Pan, Guo-Qiang Chen, Hiroaki Matsunami, Hanyi Zhuang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.5field-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

32 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Antagonists Enhance Cell-Surface Expression of Mammalian Odorant Receptors.International journal of molecular sciences · 2025
    Article
  5. Article
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  7. Article
  8. Article
  9. Review
  10. Article
  11. Interactions among key residues regulate mammalian odorant receptor trafficking.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
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  17. Article
  18. Conserved C-terminal motifs in odorant receptors instruct their cell surface expression and cAMP signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  19. Structural instability and divergence from conserved residues underlie intracellular retention of mammalian odorant receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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 3 institutions in 2 countries.

Lifang WuDepartment of Pathophysiology, Shanghai Universities E-Institute for Chemical Biology, Key Laboratory of Cell Differentiation and Apoptosis of National Ministry of Education, Shanghai Jiaotong University School of Medicine, Shanghai 200025, China.
Yi Pan
Guo-Qiang Chen
Hiroaki Matsunami
Hanyi Zhuang
Deleted InstitutionShanghai Institutes for Biological Sciences · CNDuke University · US

Funding

Molecular Mechanisms Underlying Odorant RecognitionR01DC005782 · NIDCD · DUKE UNIVERSITY · PI MATSUNAMI, HIROAKI · 2002 to 2012
$3.5M
Ligand selectivity of vomeronasal receptorsR01DC010857 · NIDCD · DUKE UNIVERSITY · PI MATSUNAMI, HIROAKI · 2010 to 2014
$1.6M
NIDCD NIH HHS DC005782NIDCD NIH HHS R01 DC005782NIDCD NIH HHS R01 DC010857
6 · The paper itself

Abstract

Odorant receptor (OR) proteins are retained in the endoplasmic reticulum when heterologously expressed in cultured cells of non-olfactory origins. RTP1S is an accessory protein to mammalian ORs and facilitates their trafficking to the cell-surface membrane and ligand-induced responses in heterologous cells. The mechanism by which RTP1S promotes the functional expression of ORs remains poorly understood. To obtain a better understanding of the role(s) of RTP1S, we performed a series of structure-function analyses of RTP1S in HEK293T cells. By constructing RTP1S deletion and chimera series and subsequently introducing single-site mutations into the protein, we found the N terminus of RTP1S is important for the endoplasmic reticulum exit of ORs and that a middle region of RTP1S is important for OR trafficking from the Golgi to the membrane. Using sucrose gradient centrifugation, we found that the localization of RTP1S to the lipid raft microdomain is critical to the activation of ORs. Finally, in a protein-protein interaction analysis, we determined that the C terminus of RTP1S may be interacting with ORs. These findings provide new insights into the distinct roles of RTP1S in OR translocation and activation.

Indexed as

Flow CytometryHEK293 CellsHumansImmunohistochemistryLigandsMembrane MicrodomainsMembrane Transport ProteinsModels, BiologicalPlasmidsProtein Structure, TertiaryProtein TransportReceptors, G-Protein-CoupledReceptors, OdorantLigandsMembrane Transport ProteinsReceptors, G-Protein-CoupledReceptors, OdorantRTP1 protein, human

Identifiers

PMID22570474
PMCPMC3381189
OpenAlexW2095270886

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.