Related Experiment Video

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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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Ubiquitin ligases in oncogenic transformation and cancer therapy

Daniela Senft1, Jianfei Qi2, Ze'ev A Ronai1,3

  • 1Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California 92130, USA.

Nature Reviews. Cancer
|December 16, 2017
PubMed

Insights

Ubiquitin ligases (E3s) control cellular processes and are crucial in cancer. Understanding E3 roles in tumorigenesis can lead to new cancer therapies and prognostic markers.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Cellular responses to stress and DNA damage rely on ubiquitin ligases (E3s).
  • E3s regulate homeostasis, metabolism, and cell cycle progression by ubiquitylating protein substrates.
  • Ubiquitin chain topology determines substrate fate, impacting proteasomal degradation, localization, and complex assembly.

Purpose of the Study:

  • To review the roles of E3s in cancer.
  • To highlight therapeutic opportunities for E3-targeted cancer treatments.

Main Methods:

  • Literature review of oncogenic and tumor-suppressor roles of selected E3s.
  • Analysis of E3 regulation and function in tumorigenesis.

Main Results:

  • Deregulation of E3s, through genetic or epigenetic alterations, is implicated in cancer.
  • Altered E3 activity affects tumor-suppressor and oncogenic activities.
  • Selected E3s exhibit both oncogenic and tumor-suppressor functions.

Conclusions:

  • Understanding E3 mechanisms in cancer is vital for developing novel prognostic markers.
  • Targeting E3s presents a promising strategy for next-generation cancer therapies.

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