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Updated: Apr 19, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

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E3 ubiquitin ligase Skp2 as an attractive target in cancer therapy

Zhonglin Hao1, Shuang Huang1

  • 1Division of Hematology and Oncology, Department of Medicine, Medical College of Georgia, Georgia Regents University, Augusta, GA30912.

Frontiers in Bioscience (Landmark Edition)
|January 2, 2015
PubMed

Insights

Skp2, an E3 ubiquitin ligase, drives cancer progression by degrading tumor suppressors like p27. Inhibiting Skp2 shows promise for treating various cancers, especially those with mutated tumor suppressor genes.

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • E3 ubiquitin ligase Skp2 targets proteins for proteasomal degradation.
  • Skp2 regulates critical cellular processes including proliferation, DNA replication, and senescence.
  • Skp2 overexpression is linked to tumorigenesis and poor prognosis in various cancers.

Purpose of the Study:

  • To review the role of Skp2 in cancer.
  • To discuss Skp2's antagonistic relationship with p27.
  • To explore Skp2 inhibition as a cancer therapy strategy.

Main Methods:

  • Literature review of Skp2's function and involvement in cancer.
  • Analysis of Skp2's prognostic significance.
  • Summary of Skp2 inhibitor development efforts.

Main Results:

  • Skp2 overexpression is oncogenic and associated with cancer progression and survival.
  • Skp2 antagonizes the tumor suppressor p27, leading to its downregulation.
  • Skp2 suppression is a potential therapeutic strategy, particularly in cancers with mutated tumor suppressors (VHL, RB, TP53).

Conclusions:

  • Skp2 plays a critical oncogenic role in diverse malignancies.
  • Targeting Skp2 offers a promising avenue for cancer treatment.
  • Further research into Skp2 inhibitors and long-term suppression implications is warranted.

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