Evidence map›Paper›PMID 12177201›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2002

The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter.

Ana M Carneiro, Susan L Ingram, Jean-Martin Beaulieu, Ava Sweeney, Susan G Amara, Sheila M Thomas, Marc G Caron, Gonzalo E Torres

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 133 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Structure and Gating Dynamics of NaFrontiers in molecular biosciences · 2019
    Review
  7. Structural and Functional Characterization of the Interaction of Snapin with the Dopamine Transporter: Differential Modulation of Psychostimulant Actions.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018
    Article
  8. Review
  9. Review
  10. Classic Studies on the Interaction of Cocaine and the Dopamine Transporter.Clinical psychopharmacology and neuroscience : the official scientific journal of the Korean College of Neuropsychopharmacology · 2015
    Article
  11. Article
  12. Article
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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

8 authors at 3 institutions in 2 countries.

Ana M CarneiroHoward Hughes Medical Institute, Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Susan L Ingram
Jean-Martin Beaulieu
Ava Sweeney
Susan G Amara
Sheila M Thomas
Marc G Caron
Gonzalo E Torres
Howard Hughes Medical Institute · USDuke Medical Center · USBeth Israel Deaconess Medical Center · US

Funding

DOPAMINE RECEPTORS:CHARACTERIZATION/ENDOCRINE REGULATIONR01NS019576 · NINDS · DUKE UNIVERSITY · PI CARON, MARC G. · 1985 to 2007
$2.9M
Cell /molecular regulation of human dopamine transporterF32DA014150 · NIDA · DUKE UNIVERSITY · PI TORRES, GONZALO E. · 2001 to 2003
$97k
NIDA NIH HHS DA-14150NIDA NIH HHS F32 DA014150NINDS NIH HHS NS-19576NINDS NIH HHS R01 NS019576
6 · The paper itself

Abstract

The Na+/Cl--dependent dopamine transporter (DAT) is critical in terminating dopaminergic transmission by removing the transmitter away from the synapse. Several lines of evidence suggest that transporter-interacting proteins may play a role in DAT function and regulation. In this report, using the yeast two-hybrid system, we have identified a novel interaction between DAT and the multiple Lin-11, Isl-1, and Mec-3 (LIM) domain-containing adaptor protein Hic-5. This association involves the N-terminal portion of the intracellular tail of DAT and the LIM region of Hic-5. In human embryonic kidney 293 cells, Hic-5 colocalizes with DAT at polarized sites and reduces DAT uptake activity through a mechanism involving a decrease in the cell-surface levels of the transporter. A fragment of Hic-5 containing the LIM domains is sufficient to bind DAT but lacks the ability to inhibit transporter activity. In addition, the LIM fragment prevents the effect of the full-length Hic-5 on DAT localization and function. In the brain, Hic-5 protein is expressed in the cerebral cortex, hippocampus, hypothalamus, cerebellum, and striatum, suggesting a role for this protein in the nervous system. The association of the endogenous Hic-5 and DAT proteins was confirmed biochemically by coimmunoprecipitation from brain striatal extracts. Moreover, immunostaining of rat midbrain neurons in culture revealed a presynaptic colocalization of Hic-5 and DAT. Because Hic-5 has been shown to interact with several signaling molecules, including the nonreceptor protein tyrosine kinases focal adhesion kinase and Fyn, this raises the possibility that this adaptor protein may link DAT to intracellular signaling pathways.

Indexed as

Nerve Tissue ProteinsAnimalsCarrier ProteinsCell LineCytoskeletal ProteinsDNA-Binding ProteinsDopamineDopamine Plasma Membrane Transport ProteinsHumansImmunohistochemistryIntracellular Signaling Peptides and ProteinsKidneyLIM Domain ProteinsMembrane GlycoproteinsMembrane Transport ProteinsMiceCarrier ProteinsCytoskeletal ProteinsDNA-Binding ProteinsDopamineDopamine Plasma Membrane Transport ProteinsIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsSerotonin Plasma Membrane Transport ProteinsSLC6A2 protein, humanSlc6a2 protein, mouseSLC6A3 protein, humanSlc6a3 protein, mouseSLC6A4 protein, humanSlc6a4 protein, mouseSymportersTGFB1I1 protein, humanTgfb1i1 protein, mouseTgfb1i1 protein, rat

Identifiers

PMID12177201
PMCPMC6757888
OpenAlexW1652457070

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.