Evidence map›Paper›PMID 23493394›Full record

ArticleThe Journal of biological chemistry2013

Plasma membrane compartmentalization of D2 dopamine receptors.

Meenakshi Sharma, Jeremy Celver, J Christopher Octeau, Abraham Kovoor

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024
    Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Lipid Rafts and Dopamine Receptor Signaling.International journal of molecular sciences · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Regulation of monoamine transporters and receptors by lipid microdomains: implications for depression.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Meenakshi SharmaDepartment of Biomedical and Pharmaceutical Sciences, University of Rhode Island, Kingston, Rhode Island 02881, USA.
Jeremy Celver
J Christopher Octeau
Abraham Kovoor
University of Rhode Island · US

Funding

UNDERGRADUATE RESEARCH AND SEMINARSP20RR016457 · NCRR · UNIVERSITY OF RHODE ISLAND · PI ALMEIDA, KAREN H. · 2001 to 2011
$35.5M
Development of A Novel Animal Model of Tardive DyskinesiaR15MH091639 · NIMH · UNIVERSITY OF RHODE ISLAND · PI KOVOOR, ABRAHAM · 2010 to 2010
$368k
NCRR NIH HHS P20 RR016457NCRR NIH HHS P20RR016457-10NIMH NIH HHS R15 MH091639NIMH NIH HHS R15MH091639
6 · The paper itself

Abstract

Plasma membrane microcompartments could allow different signaling pathways to operate more efficiently and prevent cross-talk. We utilized a novel in-cell biotin transfer assay to demonstrate that the majority of plasma membrane-expressed D2 dopamine receptor (D2R) is microcompartmentalized within detergent-resistant structures. Conversely, a minority of D2R existed in a detergent-soluble form and interacted in a relatively unrestricted manner with other cellular proteins. The microcompartmentalization of D2R had functional consequences because dopamine-induced internalization of D2R was largely restricted to the compartmentalized receptor. The D2R-containing microcompartments did not correspond to putative detergent-resistant lipid raft structures. First, the detergent-insoluble D2R structures were significantly denser than detergent-resistant membrane fragments containing flotillin, a widely utilized lipid raft marker protein. Second, the detergent solubility of D2R was unaffected by treatment of cells with the cholesterol chelating agent, methyl-β-cyclodextrin, that is thought to disrupt lipid rafts. Finally, the in-cell biotinylation assay did not provide any evidence for the membrane compartmentalization of peptide motifs thought to target to lipid rafts. Thus, our observations form one of the first demonstrations, in living cells, of plasma membrane microcompartments defined by the ability of the compartment structure to broadly restrict the interaction of resident molecules with other cellular proteins.

Indexed as

Amino Acid MotifsAnimalsbeta-CyclodextrinsHEK293 CellsHumansMembrane MicrodomainsMembrane ProteinsMiceReceptors, Dopamine D2beta-CyclodextrinsflotillinsMembrane Proteinsmethyl-beta-cyclodextrinReceptors, Dopamine D27-Helix ReceptorArrestinCell CompartmentationDopamine ReceptorsG Protein-coupled ReceptorPlasma MembranePlasma Membrane CompartmentalizationReceptor InternalizationReceptor Regulation

Identifiers

PMID23493394
PMCPMC3642303
OpenAlexW1979527210

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.