Evidence map›Paper›PMID 7650489›Full record

ArticleThe Journal of experimental medicine1995

A role for MARCKS, the alpha isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages.

L H Allen, A Aderem

Open access · hybridAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 297 citations in OpenAlex.

  1. Article
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  8. A Comparative Analysis ofInternational journal of molecular sciences · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. MicroRNA-21 Limits Uptake ofFrontiers in cellular and infection microbiology · 2017
    Article
  13. PKC-η-MARCKS Signaling Promotes Intracellular Survival of UnopsonizedFrontiers in cellular and infection microbiology · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Immunofluorescence and confocal microscopy of neutrophils.Methods in molecular biology (Clifton, N.J.) · 2014
    Article
  19. Photoreceptor phagocytosis is mediated by phosphoinositide signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  20. Article

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

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

2 authors at 1 institution in 1 country.

L H AllenLaboratory of Signal Transduction, Rockefeller University, New York 10021, USA.
A Aderem
Rockefeller University · US

Funding

LPS REGULATION OF MACROPHAGE FUNCTIONR01AI025032 · NIAID · SEATTLE BIOMEDICAL RESEARCH INSTITUTE · PI ADEREM, ALAN A · 1987 to 2016
$6.7M
LPS REGULATION OF MACROPHAGE FUNCTIONR37AI025032 · NIAID · UNIVERSITY OF WASHINGTON · PI ADEREM, ALAN A · 1995 to 2004
$2.4M
LPS-INDUCED SIGNALLING IN MACROPHAGESF32AI008618 · NIAID · ROCKEFELLER UNIVERSITY · PI ALLEN, LEE-ANN H. · 1992 to 1994
–
NIAID NIH HHS AI08618NIAID NIH HHS AI25032
6 · The paper itself

Abstract

Myristoylated, alanine-rich C-kinase substrate (MARCKS) is a lipopolysaccharide-induced protein kinase C (PKC) substrate that has been proposed to regulate actin-membrane interactions, as well as actin structure at the membrane. We studied the distribution of MARCKS, the alpha isozyme of PKC (PKC alpha), and myosin I in lipopolysaccharide-treated peritoneal macrophages ingesting zymosan particles. MARCKS, PKC alpha, and myosin I colocalized with F-actin and talin in the cortical cytoplasm adjacent to forming phagocytic cups. After particle ingestion was completed, myosin I, F-actin, and talin were no longer enriched in the vicinity of the phagosome. By contrast, MARCKS and PKC alpha remained associated with the phagosome membrane until after acquisition of the lysosomal marker Lamp-1. Vinculin was not detected on phagosomes at any time point examined. Phagocytosis of zymosan was accompanied by rapid and sustained phosphorylation of MARCKS. Inhibitors of PKC reduced zymosan binding to the macrophage surface and blocked the focal accumulation of F-actin, talin, phosphotyrosine-containing proteins, MARCKS, and PKC alpha beneath attached particles. We propose that PKC-dependent phosphorylation is an early signal required for zymosan phagocytosis and that MARCKS and PKC alpha have a role in phagosome maturation. The colocalization of F-actin and MARCKS at the cytoplasmic face of the nascent phagosome reinforces the hypothesis that MARCKS regulates actin structure at the membrane. Our data also suggest that myosin I functions as a mechanical motor during particle uptake.

Indexed as

Intracellular Signaling Peptides and ProteinsMembrane ProteinsZymosanActinsIntracellular MembranesIsoenzymesLipopolysaccharidesMacromolecular SubstancesMacrophages, PeritonealModels, BiologicalMyosinsMyristoylated Alanine-Rich C Kinase SubstratePhagocytosisPhagosomesPhosphorylationProtein Kinase CActinsIntracellular Signaling Peptides and ProteinsIsoenzymesLipopolysaccharidesMacromolecular SubstancesMembrane ProteinsMyosinsMyristoylated Alanine-Rich C Kinase SubstrateProtein Kinase CProtein Kinase C-alphaProteinsTalinVinculinZymosan

Identifiers

PMID7650489
PMCPMC2192156
OpenAlexW2126712915

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.