Functional roles of E3 ubiquitin ligases in gastric cancer

Mingliang Wang1, Wei Dai1, Zhangyan Ke2

  • 1Department of General Surgery, The First Affiliated Hospital of Anhui Medical University, Hefei, Anhui 230032, P.R. China.

Oncology Letters
|August 11, 2020
PubMed

Insights

E3 ubiquitin ligases are crucial regulators in human cancers like gastric cancer (GC). This review highlights their roles and therapeutic potential, identifying 30 key ligases involved in GC development.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • E3 ubiquitin ligases are critical regulators of protein degradation and cellular processes.
  • Over 650 E3 ligases exist in humans, categorized into RING, HECT, and RING-in-between-RING families.
  • Dysregulation of E3 ligases is implicated in various cancers, including gastric cancer (GC).

Purpose of the Study:

  • To comprehensively review the functional roles of proteasome-related E3 ubiquitin ligases in gastric cancer.
  • To summarize the latest research on E3 ligases in GC, including their structure, classification, function, and therapeutic value.
  • To identify key E3 ligases that could serve as diagnostic markers or therapeutic targets for GC.

Main Methods:

  • Literature review of recent research on E3 ubiquitin ligases in gastric cancer.
  • Analysis of the structure, classification, and functional mechanisms of E3 ligases.
  • Evaluation of the prognostic and therapeutic implications of E3 ligases in GC.

Main Results:

  • Abnormal expression and function of numerous E3 ligases have been observed in GC.
  • Specific E3 ligases are closely associated with GC cell proliferation, invasion, and patient prognosis.
  • Thirty E3 ligases with essential roles in GC development were identified, some acting as oncogenes or tumor suppressors.

Conclusions:

  • E3 ubiquitin ligases are pivotal in regulating gastric cancer development and progression.
  • These ligases represent promising therapeutic targets for novel anti-cancer strategies in GC.
  • Further investigation into the specific roles and mechanisms of E3 ligases in GC is warranted.

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