Evidence map›Paper›PMID 25429109›Full record

ArticleThe Journal of biological chemistry2015

Arg kinase-binding protein 2 (ArgBP2) interaction with α-actinin and actin stress fibers inhibits cell migration.

Praju Vikas Anekal, Jeffery Yong, Ed Manser

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Impact of Sorbs2 dysfunction on cardiovascular diseases.Biochimica et biophysica acta. Molecular basis of disease · 2025
    Review
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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

3 authors at 2 institutions in 1 country.

Praju Vikas AnekalFrom the sGSK Group Institute of Molecular and Cell Biology (IMCB), Proteos Building, 61 Biopolis Drive, 138673 Singapore.
Jeffery YongFrom the sGSK Group Institute of Molecular and Cell Biology (IMCB), Proteos Building, 61 Biopolis Drive, 138673 Singapore.
Ed ManserFrom the sGSK Group Institute of Molecular and Cell Biology (IMCB), Proteos Building, 61 Biopolis Drive, 138673 Singapore, the Institute of Medical Biology (IMB), 8A Biomedical Grove, 06-06 Immunos Building, 138648 Singapore, and the Department of Pharmacology, National University of Singapore, 119077 Singapore ed.manser@imb.a-star.edu.sg.
Institute of Molecular and Cell Biology · SGInstitute of Medical Biology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell migration requires dynamic remodeling of the actomyosin network. We report here that an adapter protein, ArgBP2, is a component of α-actinin containing stress fibers and inhibits migration. ArgBP2 is undetectable in many commonly studied cancer-derived cell lines. COS-7 and HeLa cells express ArgBP2 (by Western analysis), but expression was detectable only in approximately half the cells by immunofluorescence. Short term clonal analysis demonstrated 0.2-0.3% of cells switch ArgBP2 expression (on or off) per cell division. ArgBP2 can have a fundamental impact on the actomyosin network: ArgBP2 positive COS-7 cells, for example, are clearly distinguishable by their denser actomyosin (stress fiber) network. ArgBP2γ binding to α-actinin appears to underlie its ability to localize to stress fibers and decrease cell migration. We map a small α-actinin binding region in ArgBP2 (residues 192-228) that is essential for these effects. Protein kinase A phosphorylation of ArgBP2γ at neighboring Ser-259 and consequent 14-3-3 binding blocks its interaction with α-actinin. ArgBP2 is known to be down-regulated in some aggressively metastatic cancers. Our work provides a biochemical explanation for the anti-migratory effect of ArgBP2.

Indexed as

Cell MovementGene Expression Regulation, Enzymologic14-3-3 ProteinsActininActinsActomyosinAdaptor Proteins, Signal TransducingAnimalsCell Line, TumorChlorocebus aethiopsColforsinCOS CellsCytoskeletonHeLa CellsHomeodomain ProteinsHumans14-3-3 ProteinsActininActinsActomyosinAdaptor Proteins, Signal TransducingColforsinHomeodomain ProteinsRNA-Binding ProteinsSORBS2 protein, human14-3-3 ProteinActininActin Stress FibersArgBP2Cell MigrationCytoskeletonProtein kinase A (PKA)Tumor Metastasis

Identifiers

PMID25429109
PMCPMC4303664
OpenAlexW2063227306

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.