Evidence map›Paper›PMID 25847498›Full record

ReviewBiochimica et biophysica acta2015

Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.

George Khelashvili, Harel Weinstein

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. 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
2.4field-weighted citation impact, top 12% 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, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  6. Review
  7. Review
  8. Regulation of monoamine transporters and receptors by lipid microdomains: implications for depression.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  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

2 authors at 1 institution in 1 country.

George KhelashviliDepartment of Physiology and Biophysics, Weill Medical College of Cornell University, New York, NY, USA. Electronic address: gek2009@med.cornell.edu.
Harel WeinsteinDepartment of Physiology and Biophysics, Weill Medical College of Cornell University, New York, NY, USA; The HRH Prince Alwaleed Bin Talal Bin Abdulaziz Alsaud Institute for Computational Biomedicine, Weill Medical College of Cornell University, New York, NY, USA.
Cornell University · US

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI NAKAMOTO, ROBERT K. · 2010 to 2017
$31.9M
STRUCTURE/FUNCTION OF THE HUMAN DOPAMINE TRANSPORTERP01DA012408 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI WEINSTEIN, HAREL · 1999 to 2015
$14.2M
Molecular mechanisms of bacterial homologs of neurotransmitter:sodium symportersR01DA017293 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI JAVITCH, JONATHAN A · 2003 to 2013
$4.9M
The dopamine transporter's lipid interactions: understanding transporter functionR01DA035263 · NIDA · VANDERBILT UNIVERSITY · PI GALLI, AURELIO, MATTHIES, HEINRICH J.G. · 2014 to 2023
$3.8M
Functional Properties of Protein Segments in Receptors and TransportersR01DA015170 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI JAVITCH, JONATHAN A, WEINSTEIN, HAREL · 2002 to 2013
$2.8M
NIDA NIH HHS 5R01DA035263NIDA NIH HHS P01 DA012408NIDA NIH HHS R01 DA015170NIDA NIH HHS R01 DA017293NIDA NIH HHS R01 DA035263NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

The physiological functions of neurotransmitter:sodium symporters (NSS) in reuptake of neurotransmitters from the synapse into the presynaptic nerve have been shown to be complemented by their involvement, together with non-plasma membrane neurotransmitter transporters, in the reverse transport of substrate (efflux) in response to psychostimulants. Recent experimental evidence implicates highly anionic phosphatidylinositol 4,5-biphosphate (PIP(2)) lipids in such functions of the serotonin (SERT) and dopamine (DAT) transporters. Thus, for both SERT and DAT, neurotransmitter efflux has been shown to be strongly regulated by the presence of PIP(2) lipids in the plasma membrane, and the electrostatic interaction of the N-terminal region of DAT with the negatively charged PIP(2) lipids. We examine the experimentally established phenotypes in a structural context obtained from computational modeling based on recent crystallographic data. The results are shown to set the stage for a mechanistic understanding of physiological actions of neurotransmitter transporters in the NSS family of membrane proteins. This article is part of a Special Issue entitled: Lipid-protein interactions.

Indexed as

Protein Structure, TertiaryDopamine Plasma Membrane Transport ProteinsHumansMembrane LipidsMembrane Transport ProteinsModels, MolecularNeurotransmitter Transport ProteinsPhosphatidylinositol 4,5-DiphosphateProtein BindingSerotonin Plasma Membrane Transport ProteinsDopamine Plasma Membrane Transport ProteinsMembrane LipidsMembrane Transport ProteinsNeurotransmitter Transport ProteinsPhosphatidylinositol 4,5-DiphosphateSerotonin Plasma Membrane Transport ProteinsAmphetamine-induced effluxCell signaling and phosphorylationContinuum mean-field theoryElectrostatic interactionsLipid segregation in the membraneMembrane composition and PIP(2) lipidsMolecular dynamicsMolecular dynamics simulationsPsychostimulant drugs of abuse

Identifiers

PMID25847498
PMCPMC4501894
OpenAlexW1981937363

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.