Evidence map›Paper›PMID 25609374›Full record

ArticleMolecular pharmacology2015

Native serotonin 5-HT2C receptors are expressed as homodimers on the apical surface of choroid plexus epithelial cells.

Katharine Herrick-Davis, Ellinor Grinde, Tara Lindsley, Milt Teitler, Filippo Mancia, Ann Cowan, Joseph E Mazurkiewicz

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Roots and early routes of neuroendocrinology.Cell and tissue research · 2025
    Review
  3. Review
  4. Article
  5. Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019
    Review
  10. Article
  11. Endogenous Serotonin 5-HTACS chemical neuroscience · 2019
    Article
  12. Review
  13. Review
  14. Article
  15. BetaBiochimica et biophysica acta. Biomembranes · 2017
    Article
  16. A short history of the 5-HTPsychopharmacology · 2017
    Review
  17. Heterodimers of serotonin receptor subtypes 2 are driven by 5-HTThe Journal of biological chemistry · 2017
    Article
  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

7 authors at 2 institutions in 1 country.

Katharine Herrick-DavisCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.) daviskh@mail.amc.edu.
Ellinor GrindeCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.).
Tara LindsleyCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.).
Milt TeitlerCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.).
Filippo ManciaCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.).
Ann CowanCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.).
Joseph E MazurkiewiczCenter for Neuropharmacology & Neuroscience, Albany Medical College, Albany, New York (K.H.-D., E.G., T.L., M.T., J.E.M.); Department of Physiology and Cellular Biophysics, Columbia University, New York, New York (F.M.); and Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut (A.C.).
Columbia University · USAlbany Medical Center Hospital · US

Funding

GPCR ArchitectureR21MH086796 · NIMH · ALBANY MEDICAL COLLEGE · PI HERRICK-DAVIS, KATHARINE · 2010 to 2011
$433k
NIMH NIH HHS R21 MH086796NIMH NIH HHS R21-MH086796
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are a prominent class of plasma membrane proteins that regulate physiologic responses to a wide variety of stimuli and therapeutic agents. Although GPCR oligomerization has been studied extensively in recombinant cells, it remains uncertain whether native receptors expressed in their natural cellular environment are monomers, dimers, or oligomers. The goal of this study was to determine the monomer/oligomer status of a native GPCR endogenously expressed in its natural cellular environment. Native 5-HT2C receptors in choroid plexus epithelial cells were evaluated using fluorescence correlation spectroscopy (FCS) with photon counting histogram (PCH). An anti-5-HT2C fragment antigen binding protein was used to label native 5-HT2C receptors. A known monomeric receptor (CD-86) served as a control for decoding the oligomer status of native 5-HT2C receptors by molecular brightness analysis. FCS with PCH revealed molecular brightness values for native 5-HT2C receptors equivalent to the molecular brightness of a homodimer. 5-HT2C receptors displayed a diffusion coefficient of 5 × 10(-9) cm(2)/s and were expressed at 32 receptors/μm(2) on the apical surface of choroid plexus epithelial cells. The functional significance and signaling capabilities of the homodimer were investigated in human embryonic kidney 293 cells using agonists that bind in a wash-resistant manner to one or both protomers of the homodimer. Whereas agonist binding to one protomer resulted in G protein activation, maximal stimulation required occupancy of both protomers. This study is the first to demonstrate the homodimeric structure of 5-HT2C receptors endogenously expressed in their native cellular environment, and identifies the homodimer as a functional signaling unit.

Indexed as

Affinity LabelsAnimalsAntibodies, MonoclonalCells, CulturedChoroid PlexusEpithelial CellsGreen Fluorescent ProteinsHEK293 CellsHumansImmunoglobulin Fab FragmentsPromoter Regions, GeneticProtein MultimerizationRadioligand AssayRats, Sprague-DawleyReceptor, Serotonin, 5-HT2CSignal TransductionAffinity LabelsAntibodies, MonoclonalGreen Fluorescent ProteinsImmunoglobulin Fab FragmentsReceptor, Serotonin, 5-HT2C

Identifiers

PMID25609374
PMCPMC4366800
OpenAlexW2170891837

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.