Evidence map›Paper›PMID 18466293›Full record

ArticleTraffic (Copenhagen, Denmark)2008

Membrane localization is critical for activation of the PICK1 BAR domain.

Kenneth L Madsen, Jacob Eriksen, Laura Milan-Lobo, Daniel S Han, Masha Y Niv, Ina Ammendrup-Johnsen, Ulla Henriksen, Vikram K Bhatia, Dimitrios Stamou, Harald H Sitte and 3 more

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

13 authors.

Kenneth L MadsenDepartment of Neuroscience and Pharmacology, Molecular Neuropharmacology Group, Center for Pharmacogenomics, The Panum Institute, University of Copenhagen, DK-2200 Copenhagen N, Denmark.
Jacob Eriksen
Laura Milan-Lobo
Daniel S Han
Masha Y Niv
Ina Ammendrup-Johnsen
Ulla Henriksen
Vikram K Bhatia
Dimitrios Stamou
Harald H Sitte
Harvey T McMahon
Harel Weinstein
Ulrik Gether

Funding

STRUCTURE/FUNCTION OF THE HUMAN DOPAMINE TRANSPORTERP01DA012408 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI WEINSTEIN, HAREL · 1999 to 2015
$14.2M
Medical Research Council MC_U105178795NIDA NIH HHS P01 DA012408NIDA NIH HHS P01 DA 12408
6 · The paper itself

Abstract

The PSD-95/Discs-large/ZO-1 homology (PDZ) domain protein, protein interacting with C kinase 1 (PICK1) contains a C-terminal Bin/amphiphysin/Rvs (BAR) domain mediating recognition of curved membranes; however, the molecular mechanisms controlling the activity of this domain are poorly understood. In agreement with negative regulation of the BAR domain by the N-terminal PDZ domain, PICK1 distributed evenly in the cytoplasm, whereas truncation of the PDZ domain caused BAR domain-dependent redistribution to clusters colocalizing with markers of recycling endosomal compartments. A similar clustering was observed both upon truncation of a short putative alpha-helical segment in the linker between the PDZ and the BAR domains and upon coexpression of PICK1 with a transmembrane PDZ ligand, including the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor GluR2 subunit, the GluR2 C-terminus transferred to the single transmembrane protein Tac or the dopamine transporter C-terminus transferred to Tac. In contrast, transfer of the GluR2 C-terminus to cyan fluorescent protein, a cytosolic protein, did not elicit BAR domain-dependent clustering. Instead, localizing PICK1 to the membrane by introducing an N-terminal myristoylation site produced BAR domain-dependent, but ligand-independent, PICK1 clustering. The data support that in the absence of PDZ ligand, the PICK1 BAR domain is inhibited through a PDZ domain-dependent and linker-dependent mechanism. Moreover, they suggest that unmasking of the BAR domain's membrane-binding capacity is not a consequence of ligand binding to the PDZ domain per se but results from, and coincides with, recruitment of PICK1 to a membrane compartment.

Indexed as

Gene Expression RegulationAnimalsBiological TransportCarrier ProteinsCell MembraneChlorocebus aethiopsCOS CellsCytoskeletal ProteinsHippocampusLigandsLipidsModels, BiologicalNuclear ProteinsProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryCarrier ProteinsCytoskeletal ProteinsLigandsLipidsNuclear ProteinsPICK1 protein, rat

Identifiers

PMID18466293
PMCPMC3622726

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.