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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

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SUMO-modified insulin-like growth factor 1 receptor (IGF-1R) increases cell cycle progression and cell proliferation

Yingbo Lin1, Hongyu Liu1,2, Ahmed Waraky1

  • 1Department of Oncology and Pathology, CCK R8: 04, Karolinska Institutet, Stockholm, Sweden.

Journal of Cellular Physiology
|January 24, 2017
PubMed

Insights

Nuclear localization of insulin-like growth factor 1 receptor (nIGF-1R) is linked to cancer outcomes. SUMOylation of nIGF-1R is crucial for its role in cell proliferation and gene expression, impacting cancer progression.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Signaling

Background:

  • Nuclear localization of insulin-like growth factor 1 receptor (nIGF-1R) is observed in tumor cells and associated with poor clinical outcomes.
  • The precise physiological roles of nIGF-1R within the cell nucleus remain largely undisclosed.
  • Previous research indicated that SUMOylation enables IGF-1R nuclear translocation and gene expression modulation via enhancer binding.

Purpose of the Study:

  • To investigate the role of SUMOylation in IGF-1R nuclear translocation and its impact on cell physiology.
  • To compare the effects of wild-type IGF-1R (WT) versus a SUMOylation-deficient mutant (TSM) on cell proliferation and cell cycle progression.

Main Methods:

  • Stable transfectants of wild-type IGF1R (WT) and triple-SUMO-site-mutated IGF1R (TSM) were created in igf1r knockout mouse fibroblasts.
  • Equal expression levels of IGF-1R were confirmed between R-WT and R-TSM clones.
  • Cell proliferation, nuclear translocation, and G1-S phase progression were analyzed upon IGF-1 stimulation.

Main Results:

  • Both WT and TSM IGF-1R translocated to the nucleus, with WT showing greater nuclear presence.
  • R-WT cells exhibited significantly faster proliferation and G1-S phase progression compared to R-TSM cells.
  • R-WT cells showed increased expression of cyclins D1, A, and CDK2, and decreased p27, indicating cell cycle regulation.

Conclusions:

  • SUMOylation is critical for the full proliferative and cell cycle-promoting functions of nuclear IGF-1R.
  • SUMO-IGF-1R appears to influence upstream mechanisms controlling cell cycle regulators.
  • Further research is warranted to elucidate the specific SUMO-IGF-1R-dependent pathways involved in cancer progression.
Keywords:
IGF-1RSUMOylationcancercell cycleproliferation

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