Evidence map›Paper›PMID 16510715›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006

Lipid binding regulates synaptic targeting of PICK1, AMPA receptor trafficking, and synaptic plasticity.

Wenying Jin, Woo-Ping Ge, Junyu Xu, Mian Cao, Lisheng Peng, Wingho Yung, Dezhi Liao, Shumin Duan, Mingjie Zhang, Jun Xia

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

90 citing papers in PubMed, 134 citations in OpenAlex.

  1. Review
  2. Protein interacting with C-kinase 1 (PICK1) regulates synaptic function and reversal learning in a mouse model for schizophrenia.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2025
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  4. Review
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  6. Article
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  12. CaFrontiers in molecular neuroscience · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Palmitoylated Proteins in Dendritic Spine Remodeling.Frontiers in synaptic neuroscience · 2020
    Article
  17. Article
  18. Review
  19. Review
  20. Review

30 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 4 countries.

Wenying JinDepartment of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
Woo-Ping Ge
Junyu Xu
Mian Cao
Lisheng Peng
Wingho Yung
Dezhi Liao
Shumin Duan
Mingjie Zhang
Jun Xia
Hong Kong University of Science and Technology · HKInstitute for Biological Sciences · CAChinese University of Hong Kong · HKUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The targeting and surface expression of membrane proteins are critical to their functions. In neurons, synaptic targeting and surface expression of AMPA-type glutamate receptors were found to be critical for synaptic plasticity such as long-term potentiation and long-term depression (LTD). PICK1 (protein interacting with C kinase 1) is a cytosolic protein that interacts with many membrane proteins, including AMPA receptors via its PDZ (postsynaptic density-95/Discs large/zona occludens-1) domain. Its interactions with membrane proteins regulate their subcellular targeting and surface expression. However, the mechanism by which PICK1 regulates protein trafficking has not been fully elucidated. Here, we show that PICK1 directly binds to lipids, mainly phosphoinositides, via its BAR (Bin/amphiphysin/Rvs) domain. Lipid binding of the PICK1 BAR domain is positively regulated by its PDZ domain and negatively regulated by its C-terminal acidic domain. Mutation of critical residues of the PICK1 BAR domain eliminates its lipid-binding capability. Lipid binding of PICK1 controls the subcellular localization of the protein, because BAR domain mutant of PICK1 has diminished synaptic targeting compared with wild-type PICK1. In addition, the BAR domain mutant of PICK1 does not cluster AMPA receptors. Moreover, wild-type PICK1 enhances synaptic targeting of AMPA receptors, whereas the BAR domain mutant of PICK1 fails to do so. The BAR domain mutant of PICK1 loses its ability to regulate surface expression of the AMPA receptors and impairs expression of LTD in hippocampal neurons. Together, our findings indicate that the lipid binding of the PICK1 BAR domain is important for its synaptic targeting, AMPA receptor trafficking, and synaptic plasticity.

Indexed as

AnimalsAnimals, NewbornBiotinylationBlotting, WesternCarrier ProteinsCells, CulturedChlorocebus aethiopsCloning, MolecularCytoskeletal ProteinsDisks Large Homolog 4 ProteinDose-Response Relationship, DrugElectric StimulationEmbryo, MammalianGreen Fluorescent ProteinsHippocampusHumansCarrier ProteinsCytoskeletal ProteinsDisks Large Homolog 4 ProteinDlg4 protein, ratglutamate receptor ionotropic, AMPA 2Green Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsLipidsMembrane ProteinsNuclear ProteinsPhosphatidylinositolsPICK1 protein, ratReceptors, AMPA

Identifiers

PMID16510715
PMCPMC6793652
OpenAlexW2021462093

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.