Evidence map›Paper›PMID 24909165›Full record

ArticleOncogene2015

Nuclear translocation of IGF-1R via p150(Glued) and an importin-β/RanBP2-dependent pathway in cancer cells.

S Packham, D Warsito, Y Lin, S Sadi, R Karlsson, B Sehat, O Larsson

Erratum issuedAbstract read
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In one paragraph

Article in Oncogene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

45 citing papers in PubMed, 61 citations in OpenAlex.

  1. Insulin-like growth factor receptor signaling in physiology and disease.Signal transduction and targeted therapy · 2026
    Review
  2. Article
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  8. IGF-1R targeting in cancer - does sub-cellular localization matter?Journal of experimental & clinical cancer research : CR · 2023
    Review
  9. Article
  10. Review
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  12. Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

S PackhamDepartment of Oncology and Pathology, Karolinska Institutet, Stockholm, Sweden.
D WarsitoDepartment of Oncology and Pathology, Karolinska Institutet, Stockholm, Sweden.
Y LinDepartment of Oncology and Pathology, Karolinska Institutet, Stockholm, Sweden.
S SadiDepartment of Molecular Biosciences, Stockholm University, The Wenner-Gren Institute, Stockholm, Sweden.
R KarlssonDepartment of Molecular Biosciences, Stockholm University, The Wenner-Gren Institute, Stockholm, Sweden.
B SehatDepartment of Oncology and Pathology, Karolinska Institutet, Stockholm, Sweden.
O LarssonDepartment of Oncology and Pathology, Karolinska Institutet, Stockholm, Sweden.
Karolinska Institutet · SEWenner-Gren Foundations · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mounting evidence has shown that the insulin-like growth factor-1 receptor (IGF-1R) has critical roles in cancer cell growth. This has prompted pharmacological companies to develop agents targeting the receptor. Surprisingly, clinical trials using specific IGF-1R antibodies have, however, revealed disappointing results. Further understanding of the role of IGF-1R in cancer cells is therefore necessary for development of efficient therapeutic strategies. Recently, we showed that IGF-1R is sumoylated and translocated into the cell nucleus where it activates gene transcription. Several other studies have confirmed our findings and it has been reported that nuclear IGF-1R (nIGF-1R) has prognostic and predictive impact in cancer. To increase the understanding of IGF-1R in cancer cells, we here present the first study that proposes a pathway by which IGF-1R translocates into the cell nucleus. We could demonstrate that IGF-1R first associates with the dynactin subunit p150(Glued), which transports the receptor to the nuclear pore complex, where it co-localizes with importin-β followed by association with RanBP2. Sumoylation of IGF-1R seems to be required for interaction with RanBP2, which in turn may serve as the SUMO E3 ligase. In the context of sumoylation, we provided evidence that it may favor nIGF-1R accumulation by increasing the stability of the receptor. Taken together, topographic and functional interactions between dynactin, importin-β and RanBP2 are involved in nuclear translocation of IGF-1R. Our results provide new understanding of IGF-1R in cancer, which in turn may contribute to development of new therapeutic strategies.

Indexed as

Active Transport, Cell Nucleusbeta KaryopherinsCell Line, TumorCell NucleusDynactin ComplexHEK293 CellsHumansMaleMicrotubule-Associated ProteinsMolecular ChaperonesNeoplasm ProteinsNeoplasmsNuclear Pore Complex ProteinsReceptor, IGF Type 1Sumoylationbeta KaryopherinsDCTN1 protein, humanDynactin ComplexMicrotubule-Associated ProteinsMolecular ChaperonesNeoplasm ProteinsNuclear Pore Complex Proteinsran-binding protein 2Receptor, IGF Type 1

Identifiers

PMID24909165
OpenAlexW1980492996

What OpenQuestion holds

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Registered trials

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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.