Evidence map›Paper›PMID 29413521›Full record

ReviewAdvances in pharmacology (San Diego, Calif.)2018

Phosphorylation of the Amino Terminus of the Dopamine Transporter: Regulatory Mechanisms and Implications for Amphetamine Action.

Caline S Karam, Jonathan A Javitch

Open access · greenAbstract readReview
In one paragraph

Review in Advances in pharmacology (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Syntaxin 1 SerScience advances · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. 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 2 institutions in 1 country.

Caline S KaramCollege of Physicians & Surgeons, Columbia University, New York, NY, United States; Division of Molecular Therapeutics, New York State Psychiatric Institute, New York, NY, United States.
Jonathan A JavitchCollege of Physicians & Surgeons, Columbia University, New York, NY, United States; Division of Molecular Therapeutics, New York State Psychiatric Institute, New York, NY, United States. Electronic address: javitch@nyspi.columbia.edu.
Columbia University · USNew York State Psychiatric Institute

Funding

Probing mechanisms of amphetamine action at plasma membrane and vesicular transporters in vitro and in vivoR01DA041510 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI JAVITCH, JONATHAN A · 2017 to 2021
$2.7M
Delineating the genetic basis of amphetamine sensitivity using a Drosophila behavioral model Diversity SupplementU01DA042233 · NIDA · NEW YORK STATE PSYCHIATRIC INSTITUTE DBA RESEARCH FOUNDATION FOR MENTAL HYGIENE, INC · PI JAVITCH, JONATHAN A · 2016 to 2020
$2.2M
Molecular Determinants for the Action of PsychostimulantsK05DA022413 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI JAVITCH, JONATHAN A · 2007 to 2016
$1.3M
NIDA NIH HHS K05 DA022413NIDA NIH HHS R01 DA041510NIDA NIH HHS U01 DA042233
6 · The paper itself

Abstract

Amphetamines (AMPHs) are potent psychostimulants that are widely used and abused, with profound medical and societal impact. Their actions at dopaminergic neurons are thought to mediate their therapeutic efficacy as well as their liability for abuse and dependence. AMPHs target the dopamine transporter (DAT), the plasmalemmal membrane protein that mediates the inactivation of released dopamine (DA) through its reuptake. AMPHs act as substrates for DAT and are known to cause mobilization of dopamine (DA) to the cell exterior via DAT-mediated reverse transport (efflux). It has become increasingly evident that the mechanisms that regulate AMPH-induced DA efflux are distinct from those that regulate DA uptake. Central to these mechanisms is the phosphorylation of the DAT amino (N)-terminus, which has been repeatedly demonstrated to facilitate DAT-mediated DA efflux, without impacting other aspects of DAT physiology. This review aims to summarize the current status of knowledge regarding DAT N-terminal phosphorylation and its regulation by protein modulators and the membrane microenvironment. A better understanding of these mechanisms may lead to the identification of novel therapeutic approaches that interfere selectively with the pharmacological effects of AMPHs without altering the physiological function of DAT.

Indexed as

AmphetamineAnimalsCell MembraneCellular MicroenvironmentDopamineDopamine Plasma Membrane Transport ProteinsHumansPhosphorylationAmphetamineDopamineDopamine Plasma Membrane Transport ProteinsDopamine effluxKinasesLipid raftsPhosphatasesPsychostimulantsVesicular monoamine transporters

Identifiers

PMID29413521
PMCPMC6341980
OpenAlexW2765882114

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.