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SUMOylation-mediated PSME3-20S proteasomal degradation of transcription factor CP2c is crucial for cell cycle

Seung Han Son1, Min Young Kim1, Young Su Lim1

  • 1Department of Life Science and Research Institute for Natural Sciences, College of Natural Sciences, Hanyang University, Seoul 04763, Korea.

Science Advances
|January 27, 2023
PubMed

Insights

This study reveals a new way transcription factor CP2c is broken down using SUMO1, PSME3, and the 20S proteasome. This regulated degradation is essential for normal cell cycle progression.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Transcription factor CP2c (TFCP2) plays roles in cellular processes and cancer.
  • Regulatory mechanisms controlling CP2c levels are not fully understood.

Purpose of the Study:

  • To uncover a novel degradation pathway for CP2c.
  • To elucidate the biological significance of CP2c degradation in cell cycle progression.

Main Methods:

  • Investigated CP2c SUMOylation using SUMO1.
  • Examined the role of the PSME3/20S proteasome system in CP2c degradation.
  • Analyzed the interaction between CP2c, SUMO1, and PSME3.

Main Results:

  • Discovered CP2c is degraded via a SUMO1-dependent, ubiquitin-independent pathway involving PSME3 and the 20S proteasome.
  • Demonstrated that SUMOylated PSME3 can also mediate CP2c degradation.
  • Showed that timely CP2c degradation is crucial for accurate cell cycle progression.

Conclusions:

  • Revealed a unique SUMO1-mediated, uncanonical 20S proteasome degradation mechanism for CP2c.
  • Identified a mutual SUMO-SIM interaction between CP2c and PSME3 in this pathway.
  • Provided new mechanistic insights into CP2c's role in cell cycle regulation through dynamic degradation.

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