Evidence map›Paper›PMID 23652010›Full record

ArticleNature communications2013

Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth.

Luca Lignitto, Antonietta Arcella, Maria Sepe, Laura Rinaldi, Rossella Delle Donne, Adriana Gallo, Eduard Stefan, Verena A Bachmann, Maria A Oliva, Clelia Tiziana Storlazzi and 8 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

74 citing papers in PubMed, 135 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  5. Article
  6. PJA2 Suppresses Colorectal Cancer Progression by Controlling HDAC2 Degradation and Stability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
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14 more citing papers are in PubMed but not listed here.

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

18 authors at 7 institutions in 3 countries.

Luca LignittoDipartimento di Medicina Molecolare and Biotecnologie Mediche, University Federico II and IEOS-CNR, 80131 Naples, Italy.
Antonietta Arcella
Maria Sepe
Laura Rinaldi
Rossella Delle Donne
Adriana Gallo
Eduard Stefan
Verena A Bachmann
Maria A Oliva
Clelia Tiziana Storlazzi
Alberto L'Abbate
Arturo Brunetti
Sara Gargiulo
Matteo Gramanzini
Luigi Insabato
Corrado Garbi
Max E Gottesman
Antonio Feliciello
University of Naples Federico II · ITCeinge Biotecnologie Avanzate (Italy) · ITInstitute of Biostructure and Bioimaging · ITIstituto Neurologico Mediterraneo · ITUniversität Innsbruck · ATUniversity of Bari Aldo Moro · ITColumbia University Irving Medical Center · US

Funding

Austrian Science Fund FWF P 22608
6 · The paper itself

Abstract

Human glioblastoma is the most frequent and aggressive form of brain tumour in the adult population. Proteolytic turnover of tumour suppressors by the ubiquitin-proteasome system is a mechanism that tumour cells can adopt to sustain their growth and invasiveness. However, the identity of ubiquitin-proteasome targets and regulators in glioblastoma are still unknown. Here we report that the RING ligase praja2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumour-suppressor Hippo cascade. Degradation of Mob through the ubiquitin-proteasome system attenuates the Hippo cascade and sustains glioblastoma growth in vivo. Accordingly, accumulation of praja2 during the transition from low- to high-grade glioma is associated with significant downregulation of the Hippo pathway. These findings identify praja2 as a novel upstream regulator of the Hippo cascade, linking the ubiquitin proteasome system to deregulated glioblastoma growth.

Indexed as

ProteolysisSignal TransductionAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBrain NeoplasmsCell Line, TumorCell ProliferationGlioblastomaHEK293 CellsHippo Signaling PathwayHumansMaleMiceMice, NudeModels, BiologicalAdaptor Proteins, Signal TransducingMOB1A protein, humanPJA2 protein, humanProtein Serine-Threonine KinasesUbiquitin-Protein Ligases

Identifiers

PMID23652010
PMCPMC3674242
OpenAlexW1994170015

What OpenQuestion holds

Textmetadata
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.