Evidence map›Paper›PMID 22303009›Full record

ArticleThe Journal of biological chemistry2012

Protein interacting with C kinase 1 (PICK1) reduces reinsertion rates of interaction partners sorted to Rab11-dependent slow recycling pathway.

Kenneth L Madsen, Thor S Thorsen, Troels Rahbek-Clemmensen, Jacob Eriksen, Ulrik Gether

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Palmitoylated Proteins in Dendritic Spine Remodeling.Frontiers in synaptic neuroscience · 2020
    Article
  10. Article
  11. Recent Findings on AMPA Receptor Recycling.Frontiers in cellular neuroscience · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

5 authors.

Kenneth L MadsenMolecular Neuropharmacology Laboratory and Lundbeck Foundation Center for Biomembranes in Nanomedicine, Department of Neuroscience and Pharmacology, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Thor S Thorsen
Troels Rahbek-Clemmensen
Jacob Eriksen
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
NIDA NIH HHS P01 DA012408NIDA NIH HHS P01 DA 12408
6 · The paper itself

Abstract

The scaffolding protein PICK1 (protein interacting with C kinase 1) contains an N-terminal PSD-95/Discs large/ZO-1 (PDZ) domain and a central lipid-binding Bin/amphiphysin/Rvs (BAR) domain. PICK1 is thought to regulate trafficking of its PDZ binding partners but different and even opposing functions have been suggested. Here, we apply ELISA-based assays and confocal microscopy in HEK293 cells with inducible PICK1 expression to assess in an isolated system the ability of PICK1 to regulate trafficking of natural and engineered PDZ binding partners. The dopamine transporter (DAT), which primarily sorts to degradation upon internalization, did not form perinuclear clusters with PICK1, and PICK1 did not affect DAT internalization/recycling. However, transfer of the PICK1-binding DAT C terminus to the β(2)-adrenergic receptor, which sorts to recycling upon internalization, led to formation of PICK1 co-clusters in Rab11-positive compartments. Furthermore, PICK1 inhibited Rab11-mediated recycling of the receptor in a BAR and PDZ domain-dependent manner. In contrast, transfer of the DAT C terminus to the δ-opioid receptor, which sorts to degradation, did not result in PICK1 co-clusters or any change in internalization/recycling. Further support for a role of PICK1 determined by its PDZ cargo was obtained for the PICK1 interaction partner prolactin-releasing peptide receptor (GPR10). GPR10 co-localized with Rab11 and clustered with PICK1 upon constitutive internalization but co-localized with the late endosomal marker Rab7 and did not cluster with PICK1 upon agonist-induced internalization. Our data suggest a selective role of PICK1 in clustering and reducing the recycling rates of PDZ domain binding partners sorted to the Rab11-dependent recycling pathway.

Indexed as

EndocytosisProtein TransportCarrier ProteinsCell LineDopamine Plasma Membrane Transport ProteinsHumansInterleukin-2 Receptor alpha SubunitNuclear ProteinsProtein BindingProtein Interaction Domains and Motifsrab11 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsReceptors, AMPAReceptors, G-Protein-CoupledReceptors, OpioidCarrier ProteinsDopamine Plasma Membrane Transport Proteinsglutamate receptor ionotropic, AMPA 2Interleukin-2 Receptor alpha SubunitNuclear ProteinsPICk1 protein, humanPRLHR protein, humanrab11 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab GTP-Binding ProteinsReceptors, AMPAReceptors, G-Protein-CoupledReceptors, OpioidRecombinant Fusion Proteins

Identifiers

PMID22303009
PMCPMC3320979

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.