Evidence map›Paper›PMID 24529480›Full record

ArticleMolecular oncology2014

Regulation of the localisation and function of the oncogene LYRIC/AEG-1 by ubiquitination at K486 and K491.

Hayley J Luxton, Karin Barnouin, Gavin Kelly, Sarah Hanrahan, Nick Totty, David E Neal, Hayley C Whitaker

Open access · hybridAbstract read
In one paragraph

Article in Molecular oncology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. 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

7 authors at 2 institutions in 1 country.

Hayley J LuxtonUro-Oncology Research Group, Cancer Research UK Cambridge Institute, University of Cambridge, Li Ka Shing Centre, Robinson Way, Cambridge CB2 0RE, UK.
Karin BarnouinProtein Analysis and Proteomics, Cancer Research UK London Research Institute, London WC2A 3LY, UK; Protein Analysis and Proteomics, Cancer Research UK London Research Institute, Clare Hall Laboratories, South Mimms, Potters Bar EN6 3LD, UK.
Gavin KellyBioinformatics and Biostatistics, Cancer Research UK London Research Institute, London WC2A 3LY, UK.
Sarah HanrahanProtein Analysis and Proteomics, Cancer Research UK London Research Institute, London WC2A 3LY, UK.
Nick TottyProtein Analysis and Proteomics, Cancer Research UK London Research Institute, London WC2A 3LY, UK.
David E NealUro-Oncology Research Group, Cancer Research UK Cambridge Institute, University of Cambridge, Li Ka Shing Centre, Robinson Way, Cambridge CB2 0RE, UK.
Hayley C WhitakerUro-Oncology Research Group, Cancer Research UK Cambridge Institute, University of Cambridge, Li Ka Shing Centre, Robinson Way, Cambridge CB2 0RE, UK. Electronic address: Hayley.Whitaker@cruk.cam.ac.uk.
Cancer Research UK · GBUniversity of Cambridge · GB

Funding

Cancer Research UKMedical Research Council G0900871
6 · The paper itself

Abstract

The pivotal role of LYRIC/AEG-1 in malignant transformation, tumourigenesis and chemo-resistance has previously been demonstrated in different cell types and sub-cellular compartments. The localisation of LYRIC/AEG-1 appears crucial to its function and is regulated by three lysine-rich nuclear localisation signal regions, one of which was previously demonstrated to be modified by ubiquitin. Here we show that mutation of LYRIC/AEG-1 at K486 and K491 results in a loss of ubiquitination. A K486/491R double mutant that is incapable of ubiquitination shows reduced binding to the NFκB subunit p65 or importin-β resulting in a distinctive peri-nuclear localisation of LYRIC/AEG-1. We also provide evidence to suggest that TOPORS, an E3 ligase that also regulates p53 modification may be responsible for LYRIC/AEG-1 ubiquitin modification. Overall we demonstrate that specific sites of LYRIC/AEG-1 ubiquitination are essential for regulating LYRIC/AEG-1 localisation and functionally interacting proteins.

Indexed as

UbiquitinationAnimalsCell Adhesion MoleculesChlorocebus aethiopsCOS CellsHumansMembrane ProteinsPoint MutationProtein Interaction MapsRNA-Binding ProteinsUbiquitinCell Adhesion MoleculesMembrane ProteinsMTDH protein, humanRNA-Binding ProteinsUbiquitinLocalisationOncogeneProtein–protein interactionUbiquitin

Identifiers

PMID24529480
PMCPMC4013555
OpenAlexW2167969633

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.