Evidence map›Paper›PMID 28102201›Full record

ArticleNature communications2017

Direct PIP

Andreas Anderluh, Tina Hofmaier, Enrico Klotzsch, Oliver Kudlacek, Thomas Stockner, Harald H Sitte, Gerhard J Schütz

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Serotonin Signaling through Lipid Membranes.ACS chemical neuroscience · 2024
    Review
  13. Review
  14. Review
  15. Oligomerization of Monoamine Transporters.Sub-cellular biochemistry · 2024
    Review
  16. Review
  17. Review
  18. Structures and membrane interactions of native serotonin transporter in complexes with psychostimulants.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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 3 institutions in 2 countries.

Andreas AnderluhInstitute of Applied Physics, TU Wien, Wiedner Hauptstrasse 8-10, Vienna 1040, Austria.
Tina HofmaierCenter for Physiology and Pharmacology, Institute of Pharmacology, Medical University Vienna, Waehringerstrasse 13A, Vienna 1090, Austria.
Enrico KlotzschEMBL Australia Node in Single Molecule Science, School of Medical Sciences, ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales, Sydney, New South Wales 2052, Australia.ORCID 0000-0002-7577-9042
Oliver KudlacekCenter for Physiology and Pharmacology, Institute of Pharmacology, Medical University Vienna, Waehringerstrasse 13A, Vienna 1090, Austria.
Thomas StocknerCenter for Physiology and Pharmacology, Institute of Pharmacology, Medical University Vienna, Waehringerstrasse 13A, Vienna 1090, Austria.
Harald H SitteCenter for Physiology and Pharmacology, Institute of Pharmacology, Medical University Vienna, Waehringerstrasse 13A, Vienna 1090, Austria.ORCID 0000-0002-1339-7444
Gerhard J SchützInstitute of Applied Physics, TU Wien, Wiedner Hauptstrasse 8-10, Vienna 1040, Austria.
Medical University of Vienna · ATTU Wien · ATUNSW Sydney · AU

Funding

Austrian Science Fund FWF F 3506Austrian Science Fund FWF F 3519Austrian Science Fund FWF F 3524Austrian Science Fund FWF W 1232
6 · The paper itself

Abstract

The human serotonin transporter (hSERT) mediates uptake of serotonin from the synaptic cleft and thereby terminates serotonergic signalling. We have previously found by single-molecule microscopy that SERT forms stable higher-order oligomers of differing stoichiometry at the plasma membrane of living cells. Here, we report that SERT oligomer assembly at the endoplasmic reticulum (ER) membrane follows a dynamic equilibration process, characterized by rapid exchange of subunits between different oligomers, and by a concentration dependence of the degree of oligomerization. After trafficking to the plasma membrane, however, the SERT stoichiometry is fixed. Stabilization of the oligomeric SERT complexes is mediated by the direct binding to phosphoinositide phosphatidylinositol-4,5-biphosphate (PIP

Indexed as

AnimalsCHO CellsCricetulusEndoplasmic ReticulumGene Expression RegulationPhosphoinositide Phospholipase CSerotonin Plasma Membrane Transport ProteinsPhosphoinositide Phospholipase CSerotonin Plasma Membrane Transport Proteins

Identifiers

PMID28102201
PMCPMC5253637
OpenAlexW2579463126

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.