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Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols
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Ubiquitin ligases and cell cycle control.

Leonardo K Teixeira1, Steven I Reed

  • 1Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Annual Review of Biochemistry
|March 19, 2013
PubMed
Summary

The ubiquitin-proteasome system regulates cell division and genome stability through E3 ubiquitin ligases. This complex system also controls peripheral cell cycle processes, highlighting its broad regulatory roles.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The ubiquitin-proteasome system (UPS) is crucial for cell cycle progression and genome integrity.
  • Key regulators include Skp/cullin/F-box-containing and anaphase-promoting complex/cyclosome (APC/C) complexes.
  • Ubiquitylation extends beyond core cell cycle control, impacting peripheral processes.

Purpose of the Study:

  • To elucidate the multifaceted roles of the ubiquitin-proteasome system in cell cycle regulation.
  • To highlight the involvement of various ubiquitin ligases in maintaining cellular homeostasis and dynamicity.
  • To underscore the expanding understanding of ubiquitylation's complexity in cell cycle control.

Main Methods:

  • Review of existing literature on ubiquitin-proteasome system and cell cycle regulation.

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  • Analysis of the functions of E3 ubiquitin ligases, including SCF and APC/C complexes.
  • Exploration of ubiquitylation's role in peripheral cell cycle events.

    • Main Results:

    • The UPS is essential for the core oscillator driving the eukaryotic cell cycle.
    • Ubiquitin-mediated proteolysis by SCF and APC/C complexes maintains genome integrity.
    • Numerous other ubiquitin ligases and regulators participate in peripheral cell cycle processes.

    Conclusions:

    • The ubiquitin-proteasome system is a central regulator of cell division and genome stability.
    • Beyond core functions, ubiquitylation governs diverse signaling, homeostasis, and dynamic processes in the cell cycle.
    • The complexity and diversity of UPS regulation in cell cycle control are increasingly recognized.