Evidence map›Paper›PMID 22955285›Full record

ArticleThe Journal of biological chemistry2012

Actopaxin (α-parvin) phosphorylation is required for matrix degradation and cancer cell invasion.

Jeanine Pignatelli, Sara E LaLonde, David P LaLonde, Dominic Clarke, Christopher E Turner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Decoding Rho GTPase signalling networks in directed cell migration.Frontiers in cell and developmental biology · 2026
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  2. Macrophage Actin Cytoskeleton in Chronic Rejection.Results and problems in cell differentiation · 2026
    Review
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  6. CHILKBP protects against podocyte injury by preserving ZO-1 expression.Cellular and molecular life sciences : CMLS · 2022
    Article
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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

5 authors at 3 institutions in 1 country.

Jeanine PignatelliDepartment of Cell and Developmental Biology, State University of New York, Upstate Medical University, Syracuse, New York 13210, USA.
Sara E LaLonde
David P LaLonde
Dominic Clarke
Christopher E Turner
SUNY Upstate Medical University · USCornell University · USNew York State College of Veterinary Medicine · US

Funding

STRUCTURE AND FUNCTION OF PAXILLINR01GM047607 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 1996 to 2017
$5.5M
ILK-Actopaxin Interactions in Cell SignalingR01HL070244 · NHLBI · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 2002 to 2010
$3.0M
NHLBI NIH HHS R01 HL070244NHLBI NIH HHS R01HL070244NIGMS NIH HHS R01 GM047607NIGMS NIH HHS R01GM47607
6 · The paper itself

Abstract

Dysregulation of cell adhesion and motility is known to be an important factor in the development of tumor malignancy. Actopaxin (α-parvin) is a paxillin, integrin-linked kinase, and F-actin binding focal adhesion protein with several serine phosphorylation sites in the amino terminus that contribute to the regulation of cell spreading and migration. Here, phosphorylation of actopaxin is shown to contribute to the regulation of matrix degradation and cell invasion. Osteosarcoma cells stably expressing wild type (WT), nonphosphorylatable (Quint), and phosphomimetic (S4D/S8D) actopaxin demonstrate that actopaxin phosphorylation is necessary for efficient Src and matrix metalloproteinase-driven degradation of extracellular matrix. Rac1 was found to be required for actopaxin-induced matrix degradation whereas inhibition of myosin contractility promoted degradation in the phosphomutant-expressing Quint cells, indicating that a balance of Rho GTPase signaling and regulation of cellular tension are important for the process. Furthermore, actopaxin forms a complex with the Rac1/Cdc42 GEF β-PIX and Rac1/Cdc42 effector PAK1, to regulate actopaxin-dependent matrix degradation. Actopaxin phosphorylation is elevated in the invasive breast cancer cell line MDA-MB-231 compared with normal breast epithelial MCF10A cells. Expression of the nonphosphorylatable Quint actopaxin in MDA-MB-231 cells inhibits cell invasion whereas overexpression of WT actopaxin promotes invasion in MCF10A cells. Taken together, this study demonstrates a new role for actopaxin phosphorylation in matrix degradation and cell invasion via regulation of Rho GTPase signaling.

Indexed as

Protein Processing, Post-TranslationalProteolysisCalponinsCell Line, TumorCell MovementEnzyme InhibitorsExtracellular MatrixGuanine Nucleotide Exchange FactorsHumansMatrix Metalloproteinases, SecretedMicrofilament ProteinsMyosinsNeoplasm InvasivenessNeoplasmsp21-Activated Kinasesp38 Mitogen-Activated Protein KinasesARHGEF7 protein, humanCalponinsEnzyme InhibitorsGuanine Nucleotide Exchange FactorsMatrix Metalloproteinases, SecretedMicrofilament ProteinsMyosinsp21-Activated Kinasesp38 Mitogen-Activated Protein KinasesPARVA protein, humanrac1 GTP-Binding ProteinRAC1 protein, humanRho Guanine Nucleotide Exchange Factorssrc-Family Kinases

Identifiers

PMID22955285
PMCPMC3481328
OpenAlexW2020627520

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.