Evidence map›Paper›PMID 27437940›Full record

ArticlePloS one2016

ASPP2 Is a Novel Pan-Ras Nanocluster Scaffold.

Itziar M D Posada, Marc Serulla, Yong Zhou, Christina Oetken-Lindholm, Daniel Abankwa, Benoît Lectez

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. FLIM-FRET Analysis of Ras Nanoclustering and Membrane-Anchorage.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  7. Ras Variant Biology and Contributions to Human Disease.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Expression and significance of ASPP2 in squamous carcinoma of esophagus.The Kaohsiung journal of medical sciences · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Article
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 2 countries.

Itziar M D PosadaTurku Centre for Biotechnology, Åbo Akademi University, Tykistökatu 6B, 20520, Turku, Finland.
Marc SerullaTurku Centre for Biotechnology, Åbo Akademi University, Tykistökatu 6B, 20520, Turku, Finland.
Yong ZhouUniversity of Texas Health Science Center at Houston, Medical School, Houston, Texas, United States of America.
Christina Oetken-LindholmTurku Centre for Biotechnology, Åbo Akademi University, Tykistökatu 6B, 20520, Turku, Finland.
Daniel AbankwaTurku Centre for Biotechnology, Åbo Akademi University, Tykistökatu 6B, 20520, Turku, Finland.ORCID http://orcid.org/0000-0003-2769-0745
Benoît LectezTurku Centre for Biotechnology, Åbo Akademi University, Tykistökatu 6B, 20520, Turku, Finland.
Åbo Akademi University · FIThe University of Texas Health Science Center at Houston · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ras-induced senescence mediated through ASPP2 represents a barrier to tumour formation. It is initiated by ASPP2's interaction with Ras at the plasma membrane, which stimulates the Raf/MEK/ERK signaling cascade. Ras to Raf signalling requires Ras to be organized in nanoscale signalling complexes, called nanocluster. We therefore wanted to investigate whether ASPP2 affects Ras nanoclustering. Here we show that ASPP2 increases the nanoscale clustering of all oncogenic Ras isoforms, H-ras, K-ras and N-ras. Structure-function analysis with ASPP2 truncation mutants suggests that the nanocluster scaffolding activity of ASPP2 converges on its α-helical domain. While ASPP2 increased effector recruitment and stimulated ERK and AKT phosphorylation, it did not increase colony formation of RasG12V transformed NIH/3T3 cells. By contrast, ASPP2 was able to suppress the transformation enhancing ability of the nanocluster scaffold Gal-1, by competing with the specific effect of Gal-1 on H-rasG12V- and K-rasG12V-nanoclustering, thus imposing ASPP2's ERK and AKT signalling signature. Similarly, ASPP2 robustly induced senescence and strongly abrogated mammosphere formation irrespective of whether it was expressed alone or together with Gal-1, which by itself showed the opposite effect in Ras wt or H-ras mutant breast cancer cells. Our results suggest that Gal-1 and ASPP2 functionally compete in nanocluster for active Ras on the plasma membrane. ASPP2 dominates the biological outcome, thus switching from a Gal-1 supported growth-promoting setting to a senescence inducing and stemness suppressive program in cancer cells. Our results support Ras nanocluster as major integrators of tumour fate decision events.

Indexed as

AnimalsApoptosisCarcinogenesisCell MembraneCell Transformation, NeoplasticCellular SenescenceGene Expression Regulation, NeoplasticHumansMAP Kinase Signaling SystemMCF-7 CellsMiceNeoplasmsNIH 3T3 CellsOncogene Protein v-aktProto-Oncogene Proteins p21(ras)raf KinasesHras protein, mouseOncogene Protein v-aktProto-Oncogene Proteins p21(ras)raf Kinasesras ProteinsTrp53bp2 protein, mouseTumor Suppressor Proteins

Identifiers

PMID27437940
PMCPMC4954646
OpenAlexW2484090246

What OpenQuestion holds

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LicenceCC BY
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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.