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Updated: Jun 12, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

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

Published on: May 10, 2022

Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells

Seung H Choi1, Jason B Wright, Scott A Gerber

  • 1Department of Genetics, Dartmouth Medical School, Norris Cotton Cancer Center, Lebanon, New Hampshire 03756, USA.

Genes & Development
|June 17, 2010
PubMed

Insights

A newly discovered protein, TRPC4AP/TRUSS, targets Myc for degradation, crucial for cell growth. Its reduced expression in cancer stabilizes Myc, promoting tumor growth.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Cancer Research

Background:

  • Myc protein turnover is essential for normal cell growth and response to signals.
  • Dysregulation of Myc contributes to cancer development.

Purpose of the Study:

  • To identify and characterize novel regulators of Myc protein degradation.
  • To investigate the role of TRPC4AP/TRUSS in Myc regulation and cancer.

Main Methods:

  • Protein-protein interaction studies to identify Myc-binding partners.
  • Ubiquitination assays to assess Myc modification.
  • Cell-based assays to evaluate Myc transactivation and transformation.
  • Analysis of TRPC4AP/TRUSS expression in cancer cell lines.

Main Results:

  • TRPC4AP/TRUSS, a receptor for a DDB1-CUL4 E3 ligase complex, selectively degrades Myc via the proteasome.
  • TRPC4AP/TRUSS binds Myc and promotes its ubiquitination and destruction.
  • TRPC4AP/TRUSS suppresses Myc-driven transactivation and transformation.
  • TRPC4AP/TRUSS expression is significantly downregulated in most cancer cell lines, leading to Myc stabilization.

Conclusions:

  • TRPC4AP/TRUSS represents a novel pathway for Myc degradation.
  • The suppression of this pathway in cancer contributes to Myc protein stabilization and oncogenesis.

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