Evidence map›Paper›PMID 23029259›Full record

ArticlePloS one2012

GAGE cancer-germline antigens are recruited to the nuclear envelope by germ cell-less (GCL).

Morten F Gjerstorff, Heike I Rösner, Christina B Pedersen, Katrine B V Greve, Steffen Schmidt, Katherine L Wilson, Jan Mollenhauer, Hüseyin Besir, Flemming M Poulsen, Niels Erik Møllegaard and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Emerin deficiency drives MCF7 cells to an invasive phenotype.bioRxiv : the preprint server for biology · 2024
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  4. Review
  5. Review
  6. Article
  7. The Role of Emerin in Cancer Progression and Metastasis.International journal of molecular sciences · 2021
    Review
  8. Diseases of the Nucleoskeleton.Comprehensive Physiology · 2016
    Review
  9. Article
  10. Article
  11. Emerin in health and disease.Seminars in cell & developmental biology · 2014
    Review
  12. Review
  13. Review
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

11 authors at 4 institutions in 2 countries.

Morten F GjerstorffDepartment of Cancer and Inflammation Research, Institute for Molecular Medicine, University of Southern Denmark, Odense, Denmark. mgjerstorff@health.sdu.dk
Heike I Rösner
Christina B Pedersen
Katrine B V Greve
Steffen Schmidt
Katherine L Wilson
Jan Mollenhauer
Hüseyin Besir
Flemming M Poulsen
Niels Erik Møllegaard
Henrik J Ditzel
University of Southern Denmark · DKUniversity of Copenhagen · DKJohns Hopkins Medicine · USMolecular Research Institute · US

Funding

REGULATION OF NUCLEAR ENVELOPE ASSEMBLY AND DISASSEMBLYR01GM048646 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WILSON, KATHERINE L · 1994 to 2012
$4.9M
NIGMS NIH HHS R01 GM048646NIGMS NIH HHS R01 GM48646
6 · The paper itself

Abstract

GAGE proteins are highly similar, primate-specific molecules with unique primary structure and undefined cellular roles. They are restricted to cells of the germ line in adult healthy individuals, but are broadly expressed in a wide range of cancers. In a yeast two-hybrid screen we identified the metazoan transcriptional regulator, Germ cell-less (GCL), as an interaction partner of GAGE12I. GCL directly binds LEM-domain proteins (LAP2β, emerin, MAN1) at the nuclear envelope, and we found that GAGE proteins were recruited to the nuclear envelope inner membrane by GCL. Based on yeast two-hybrid analysis and pull-down experiments of GCL polypeptides, GCL residues 209-320 (which includes the BACK domain) were deduced sufficient for association with GAGE proteins. GAGE mRNAs and GCL mRNA were demonstrated in human testis and most types of cancers, and at the protein level GAGE members and GCL were co-expressed in cancer cell lines. Structural studies of GAGE proteins revealed no distinct secondary or tertiary structure, suggesting they are intrinsically disordered. Interestingly GAGE proteins formed stable complexes with dsDNA in vitro at physiological concentrations, and GAGE12I bound several different dsDNA fragments, suggesting sequence-nonspecific binding. Dual association of GAGE family members with GCL at the nuclear envelope inner membrane in cells, and with dsDNA in vitro, implicate GAGE proteins in chromatin regulation in germ cells and cancer cells.

Indexed as

Antigens, NeoplasmCell LineCell Transformation, NeoplasticChromatinCircular DichroismDNAElectrophoretic Mobility Shift AssayGene ExpressionHumansMaleNeoplasm ProteinsNuclear EnvelopeOrgan SpecificityPlasmidsProtein BindingProtein Structure, SecondaryAntigens, NeoplasmChromatinDNAGAGE7 protein, humanGMCL1 protein, humanNeoplasm ProteinsTranscription Factors

Identifiers

PMID23029259
PMCPMC3447759
OpenAlexW2021999625

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.