Evidence map›Paper›PMID 9647646›Full record

ArticleThe Journal of cell biology1998

G protein beta subunit-null mutants are impaired in phagocytosis and chemotaxis due to inappropriate regulation of the actin cytoskeleton.

B Peracino, J Borleis, T Jin, M Westphal, J M Schwartz, L Wu, E Bracco, G Gerisch, P Devreotes, S Bozzaro

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 131 citations in OpenAlex.

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  12. Regulation of Chemokine Signal Integration by Activator of G-Protein Signaling 4 (AGS4).The Journal of pharmacology and experimental therapeutics · 2017
    Article
  13. Chemical and mechanical stimuli act on common signal transduction and cytoskeletal networks.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
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  17. Ionic imbalance, in addition to molecular crowding, abates cytoskeletal dynamics and vesicle motility during hypertonic stress.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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

10 authors at 3 institutions in 2 countries.

B PeracinoDipartimento di Scienze Cliniche e Biologiche, Università di Torino, Ospedale S. Luigi, 10043 Orbassano, Italy.
J Borleis
T Jin
M Westphal
J M Schwartz
L Wu
E Bracco
G Gerisch
P Devreotes
S Bozzaro
Johns Hopkins University · USKalVista Pharmaceuticals (United States) · USMax Planck Institute of Biochemistry · DE

Funding

Signaling Networks in Chemotaxis and CytokinesisR37GM028007 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI DEVREOTES, PETER N · 2005 to 2014
$6.3M
SIGNAL TRANSDUCTION AND DICTYOSTELIUM DEVELOPMENTR01GM028007 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI DEVREOTES, PETER N · 1985 to 2004
$2.4M
NIGMS NIH HHS GM 28007NIGMS NIH HHS R01 GM028007NIGMS NIH HHS R37 GM028007
6 · The paper itself

Abstract

Chemotaxis and phagocytosis are basically similar in cells of the immune system and in Dictyostelium amebae. Deletion of the unique G protein beta subunit in D. discoideum impaired phagocytosis but had little effect on fluid-phase endocytosis, cytokinesis, or random motility. Constitutive expression of wild-type beta subunit restored phagocytosis and normal development. Chemoattractants released by cells or bacteria trigger typical transient actin polymerization responses in wild-type cells. In beta subunit-null cells, and in a series of beta subunit point mutants, these responses were impaired to a degree that correlated with the defect in phagocytosis. Image analysis of green fluorescent protein-actin transfected cells showed that beta subunit- null cells were defective in reshaping the actin network into a phagocytic cup, and eventually a phagosome, in response to particle attachment. Our results indicate that signaling through heterotrimeric G proteins is required for regulating the actin cytoskeleton during phagocytic uptake, as previously shown for chemotaxis. Inhibitors of phospholipase C and intracellular Ca2+ mobilization inhibited phagocytosis, suggesting the possible involvement of these effectors in the process.

Indexed as

ActinsAnimalsCell DivisionCell MovementChemotactic FactorsChemotaxisCytoskeletonDictyosteliumEscherichia coliGTP-Binding ProteinsMutagenesisPhagocytosisPinocytosisSalmonellaSignal TransductionActinsChemotactic FactorsGTP-Binding Proteins

Identifiers

PMID9647646
PMCPMC2133009
OpenAlexW2159113211

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.