Evidence map›Paper›PMID 11739781›Full record

ArticleMolecular biology of the cell2001

The NH(2)-terminus of norepinephrine transporter contains a basolateral localization signal for epithelial cells.

H H Gu, X Wu, B Giros, M G Caron, M J Caplan, G Rudnick

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 37 citations in OpenAlex.

  1. Life and Death of Fungal Transporters under the Challenge of Polarity.International journal of molecular sciences · 2020
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Chloride requirement for monoamine transporters.Pflugers Archiv : European journal of physiology · 2016
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Trafficking of dopamine transporters in psychostimulant actions.Seminars in cell & developmental biology · 2009
    Review
  13. Article
  14. Article
  15. Serotonin transporters--structure and function.The Journal of membrane biology · 2006
    Review
  16. Review
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

6 authors at 2 institutions in 1 country.

H H GuDepartment of Pharmacology, Yale University, New Haven, CT 06510, USA.
X Wu
B Giros
M G Caron
M J Caplan
G Rudnick
Howard Hughes Medical Institute · USYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When expressed in epithelial cells, dopamine transporter (DAT) was detected predominantly in the apical plasma membrane, whereas norepinephrine transporter (NET) was found in the basolateral membrane, despite 67% overall amino acid sequence identity. To identify possible localization signals responsible for this difference, DAT-NET chimeras were expressed in MDCK cells and localized by immunocytochemistry and transport assays. The results suggested that localization of these transporters in MDCK cells depends on their highly divergent NH(2)-terminal regions. Deletion of the first 58 amino acids of DAT (preceding TM1) did not change its apical localization. However, the replacement of that region with corresponding sequence from NET resulted in localization of the chimeric protein to the basolateral membrane, suggesting that the NH(2)-terminus of NET, which contains two dileucine motifs, contains a basolateral localization signal. Mutation of these leucines to alanines in the context of a basolaterally localized NET/DAT chimera restored transporter localization to the apical membrane, indicating that the dileucine motifs are critical to the basolateral localization signal embodied within the NET NH(2)-terminal region. However, the same mutation in the context of wild-type NET did not disrupt basolateral localization, indicating the presence of additional signals in NET directing its basolateral localization within the plasma membrane.

Indexed as

Cell PolarityMembrane GlycoproteinsNerve Tissue ProteinsAmino Acid SequenceAnimalsCell LineDogsDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansMembrane Transport ProteinsMiceMicroscopy, ConfocalMolecular Sequence DataMutagenesis, Site-DirectedNorepinephrine Plasma Membrane Transport ProteinsDopamine Plasma Membrane Transport ProteinsMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsProtein Sorting SignalsSLC6A2 protein, humanSlc6a2 protein, mouseSLC6A3 protein, humanSlc6a3 protein, mouseSymporters

Identifiers

PMID11739781
PMCPMC60756
OpenAlexW2157523820

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.