Evidence map›Paper›PMID 20147288›Full record

ArticleThe Journal of biological chemistry2010

Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons.

Heidi Q Xie, Dong Liang, K Wing Leung, Vicky P Chen, Kevin Y Zhu, Wallace K B Chan, Roy C Y Choi, Jean Massoulié, Karl W K Tsim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
5.4field-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

28 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. A Structured Brain-wide and Genome-wide Association Study Using ADNI PET Images.The Canadian journal of statistics = Revue canadienne de statistique · 2021
    Article
  4. Interacting withActa pharmaceutica Sinica. B · 2020
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  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

9 authors at 3 institutions in 2 countries.

Heidi Q XieDepartment of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Clear Water Bay Road, Kowloon, Hong Kong.
Dong Liang
K Wing Leung
Vicky P Chen
Kevin Y Zhu
Wallace K B Chan
Roy C Y Choi
Jean Massoulié
Karl W K Tsim
Hong Kong University of Science and Technology · HKUniversity of Hong Kong · HKLaboratoire de Géologie de l’École Normale Supérieure · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the mammalian brain, acetylcholinesterase (AChE) is anchored in cell membranes by a transmembrane protein PRiMA (proline-rich membrane anchor). We present evidence that at least part of the PRiMA-linked AChE is integrated in membrane microdomains called rafts. A significant proportion of PRiMA-linked AChE tetramers from rat brain was recovered in raft fractions; this proportion was markedly higher at low rather than at high concentrations of cold Triton X-100. The detergent-resistant fraction increased during brain development. In NG108-15 neuroblastoma cells transfected with cDNAs encoding AChE(T) and PRiMA, PRiMA-linked G(4) AChE was found in membrane rafts and showed the same sensitivity to cold Triton X-100 extraction as in the brain. The association of PRiMA-linked AChE with rafts was weaker than that of glycosylphosphatidylinositol-anchored G(2) AChE or G(4) Q(N)-H(C)-linked AChE. It was found to depend on the presence of a cholesterol-binding motif, called CRAC (cholesterol recognition/interaction amino acid consensus), located at the junction of transmembrane and cytoplasmic domains of both PRiMA I and II isoforms. The cytoplasmic domain of PRiMA, which differs between PRiMA I and PRiMA II, appeared to play some role in stabilizing the raft localization of G(4) AChE, because the Triton X-100-resistant fraction was smaller with the shorter PRiMA II isoform than that with the longer PRiMA I isoform.

Indexed as

AcetylcholinesteraseAmino Acid MotifsAmino Acid SequenceAnimalsBrainHumansMaleMembrane MicrodomainsMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsNeuronsProlineRatsRats, Sprague-DawleySequence Homology, Amino AcidAcetylcholinesteraseMembrane ProteinsNerve Tissue ProteinsPRIMA1 protein, humanPRiMA1 protein, ratProline

Identifiers

PMID20147288
PMCPMC2857032
OpenAlexW1964713456

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.