Evidence map›Paper›PMID 26945059›Full record

ArticleJournal of cell science2016

PP2A binds to the LIM domains of lipoma-preferred partner through its PR130/B″ subunit to regulate cell adhesion and migration.

Veerle Janssens, Karen Zwaenepoel, Carine Rossé, Marleen M R Petit, Jozef Goris, Peter J Parker

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2016. 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
1.9field-weighted citation impact, top 17% 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, 28 citations in OpenAlex.

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  12. [Overexpression of protein phosphatase 2 regulatory subunit B''α gene effect on proliferation and invasion of hepatoma cells].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2019
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  17. Emerging roles for LPP in metastatic cancer progression.Journal of cell communication and signaling · 2018
    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

6 authors at 2 institutions in 3 countries.

Veerle JanssensFrancis Crick Institute, Protein Phosphorylation Laboratory, 44 Lincoln's Inn Fields, London WC2A 3PX, UK Laboratory of Protein Phosphorylation and Proteomics, Dept. of Cellular and Molecular Medicine, KU Leuven, Herestraat 49 PO-box 901, Leuven B-3000, Belgium veerle.janssens@med.kuleuven.be peter.parker@crick.ac.uk.ORCID http://orcid.org/0000-0002-6772-8448
Karen ZwaenepoelLaboratory of Protein Phosphorylation and Proteomics, Dept. of Cellular and Molecular Medicine, KU Leuven, Herestraat 49 PO-box 901, Leuven B-3000, Belgium.
Carine RosséFrancis Crick Institute, Protein Phosphorylation Laboratory, 44 Lincoln's Inn Fields, London WC2A 3PX, UK Research Centre, Institut Curie, Paris 75005, France.
Marleen M R PetitMolecular Oncology Laboratory, Dept. of Human Genetics, KU Leuven, Herestraat 49 PO-box 602, Leuven B-3000, Belgium.ORCID http://orcid.org/0000-0003-4557-0245
Jozef GorisLaboratory of Protein Phosphorylation and Proteomics, Dept. of Cellular and Molecular Medicine, KU Leuven, Herestraat 49 PO-box 901, Leuven B-3000, Belgium.
Peter J ParkerFrancis Crick Institute, Protein Phosphorylation Laboratory, 44 Lincoln's Inn Fields, London WC2A 3PX, UK Division of Cancer Studies King's College London, Guy's Hospital Campus, Thomas Street, London SE1 9RT, UK veerle.janssens@med.kuleuven.be peter.parker@crick.ac.uk.
KU Leuven · BEThe Honourable Society of Lincoln's Inn · GB

Funding

Cancer Research UK 15683Medical Research Council FC001130
6 · The paper itself

Abstract

Here, we identify the LIM protein lipoma-preferred partner (LPP) as a binding partner of a specific protein phosphatase 2A (PP2A) heterotrimer that is characterised by the regulatory PR130/B″α1 subunit (encoded by PPP2R3A). The PR130 subunit interacts with the LIM domains of LPP through a conserved Zn²⁺-finger-like motif in the differentially spliced N-terminus of PR130. Isolated LPP-associated PP2A complexes are catalytically active. PR130 colocalises with LPP at multiple locations within cells, including focal contacts, but is specifically excluded from mature focal adhesions, where LPP is still present. An LPP-PR130 fusion protein only localises to focal adhesions upon deletion of the domain of PR130 that binds to the PP2A catalytic subunit (PP2A/C), suggesting that PR130-LPP complex formation is dynamic and that permanent recruitment of PP2A activity might be unfavourable for focal adhesion maturation. Accordingly, siRNA-mediated knockdown of PR130 increases adhesion of HT1080 fibrosarcoma cells onto collagen I and decreases their migration in scratch wound and Transwell assays. Complex formation with LPP is mandatory for these PR130-PP2A functions, as neither phenotype can be rescued by re-expression of a PR130 mutant that no longer binds to LPP. Our data highlight the importance of specific, locally recruited PP2A complexes in cell adhesion and migration dynamics.

Indexed as

Catalytic DomainCell Line, TumorCell MovementCytoskeletal ProteinsFocal AdhesionsHumansLIM Domain ProteinsProtein BindingProtein Phosphatase 2RNA, Small InterferingCytoskeletal ProteinsLIM Domain ProteinsLPP protein, humanPPP2R3A protein, humanProtein Phosphatase 2RNA, Small InterferingCell adhesionCell migrationLIM domainLipoma-preferred partnerProtein phosphatase 2AZn2+-finger

Identifiers

PMID26945059
PMCPMC5333791
OpenAlexW2292601194

What OpenQuestion holds

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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.