Evidence map›Paper›PMID 7876307›Full record

ArticleThe Journal of cell biology1995

Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods.

D Cox, J A Ridsdale, J Condeelis, J Hartwig

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 67 citations in OpenAlex.

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  12. Myosin I overexpression impairs cell migration.The Journal of cell biology · 1997
    Article
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  16. Overlapping functions of myosin-I isoforms?The Journal of cell biology · 1996
    Review
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  19. 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

4 authors at 1 institution in 1 country.

D CoxDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461.
J A Ridsdale
J Condeelis
J Hartwig
Albert Einstein College of Medicine · US

Funding

INTERACTIONS OF ACTIN CYTOSKELETON WITH PLASMA MEMBRANER01GM025813 · NIGMS · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 1985 to 2003
$1.5M
REGULATION OF PLATELET SHAPE CHANGESR01HL047874 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI HARTWIG, JOHN H · 1991 to 1993
–
NHLBI NIH HHS HL47874NIGMS NIH HHS 5T32 GM25813NIGMS NIH HHS GM25813
6 · The paper itself

Abstract

This study extends the observations on the defects in pseudopod formation of ABP-120+ and ABP-120- cells by a detailed morphological and biochemical analysis of the actin based cytoskeleton. Both ABP-120+ and ABP-120- cells polymerize the same amount of F-actin in response to stimulation with cAMP. However, unlike ABP-120+ cells, ABP-120- cells do not incorporate actin into the Triton X-100-insoluble cytoskeleton at 30-50 s, the time when ABP-120 is incorporated into the cytoskeleton and when pseudopods are extended after cAMP stimulation in wild-type cells. By confocal and electron microscopy, pseudopods extended by ABP-120- cells are not as large or thick as those produced by ABP-120+ cells and in the electron microscope, an altered filament network is found in pseudopods of ABP-120- cells when compared to pseudopods of ABP-120+ cells. The actin filaments found in areas of pseudopods in ABP-120+ cells either before or after stimulation were long, straight, and arranged into space filling orthogonal networks. Protrusions of ABP-120- cells are less three-dimensional, denser, and filled with multiple foci of aggregated filaments consistent with collapse of the filament network due to the absence of ABP-120-mediated cross-linking activity. The different organization of actin filaments may account for the diminished size of protrusions observed in living and fixed ABP-120- cells compared to ABP-120+ cells and is consistent with the role of ABP-120 in regulating pseudopod extension through its cross-linking of actin filaments.

Indexed as

Actin CytoskeletonActinsAmanitinsAnimalsCarrier ProteinsCyclic AMPCytoskeletonDictyosteliumGene DeletionMicrofilament ProteinsMicroscopy, ConfocalMicroscopy, ElectronMicroscopy, FluorescenceModels, BiologicalPhagocytesPolyethylene Glycols7-nitrobenz-2-oxa-1,3-diazole-phallacidinabpC protein, DictyosteliumActinsAmanitinsCarrier ProteinsCyclic AMPMicrofilament ProteinsPolyethylene Glycols

Identifiers

PMID7876307
PMCPMC2120398
OpenAlexW2105574356

What OpenQuestion holds

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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.