Evidence map›Paper›PMID 23329829›Full record

ArticleThe Journal of biological chemistry2013

Functional role of the interaction between polysialic acid and myristoylated alanine-rich C kinase substrate at the plasma membrane.

Thomas Theis, Bibhudatta Mishra, Maren von der Ohe, Gabriele Loers, Maksymilian Prondzynski, Ole Pless, Perry J Blackshear, Melitta Schachner, Ralf Kleene

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Neural glycomics: the sweet side of nervous system functions.Cellular and molecular life sciences : CMLS · 2021
    Review
  8. Polysialic Acid in the Immune System.Frontiers in immunology · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 5 institutions in 3 countries.

Thomas TheisZentrum für Molekulare Neurobiologie, Universitätsklinikum Hamburg-Eppendorf, 20246 Hamburg, Germany.
Bibhudatta Mishra
Maren von der Ohe
Gabriele Loers
Maksymilian Prondzynski
Ole Pless
Perry J Blackshear
Melitta Schachner
Ralf Kleene
Universität Hamburg · DEHamburg Port Consulting (Germany) · DENational Institutes of Health · USRutgers, The State University of New Jersey · USUniversity Medical Center Hamburg-Eppendorf · DE

Funding

TTP and related proteins in the regulation of gene expressionZIAES090080 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI BLACKSHEAR, PERRY J · 2009 to 2025
$52.6M
6 · The paper itself

Abstract

Polysialic acid (PSA) is a homopolymeric glycan that plays crucial roles in the developing and adult nervous system. So far only a few PSA-binding proteins have been identified. Here, we identify myristoylated alanine-rich C kinase substrate (MARCKS) as novel PSA binding partner. Binding assays showed a direct interaction between PSA and a peptide comprising the effector domain of MARCKS (MARCKS-ED). Co-immunoprecipitation of PSA-carrying neural cell adhesion molecule (PSA-NCAM) with MARCKS and co-immunostaining of MARCKS and PSA at the cell membrane of hippocampal neurons confirm the interaction between PSA and MARCKS. Co-localization and an intimate interaction of PSA and MARCKS at the cell surface was seen by confocal microscopy and fluorescence resonance energy transfer (FRET) analysis after the addition of fluorescently labeled PSA or PSA-NCAM to live CHO cells or hippocampal neurons expressing MARCKS as a fusion protein with green fluorescent protein (GFP). Cross-linking experiments showed that extracellularly applied PSA or PSA-NCAM and intracellularly expressed MARCKS-GFP are in close contact, suggesting that PSA and MARCKS interact with each other at the plasma membrane from opposite sides. Insertion of PSA and MARCKS-ED peptide into lipid bilayers from opposite sides alters the electric properties of the bilayer confirming the notion that PSA and the effector domain of MARCKS interact at and/or within the plane of the membrane. The MARCKS-ED peptide abolished PSA-induced enhancement of neurite outgrowth from cultured hippocampal neurons indicating an important functional role for the interaction between MARCKS and PSA in the developing and adult nervous system.

Indexed as

AnimalsCell MembraneCHO CellsCricetinaeCricetulusHippocampusIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsMiceMice, KnockoutMyristoylated Alanine-Rich C Kinase SubstrateNerve Tissue ProteinsNeural Cell Adhesion Molecule L1NeuritesPeptidesIntracellular Signaling Peptides and ProteinsLipid BilayersMarcks protein, mouseMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstrateNerve Tissue ProteinsNeural Cell Adhesion Molecule L1Peptidespolysialic acidpolysialyl neural cell adhesion moleculeSialic Acids

Identifiers

PMID23329829
PMCPMC3585110
OpenAlexW2094844863

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.