Related Experiment Video

Updated: Jun 30, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

The promiscuity of ARF interactions with the proteasome

Alessandra Pollice1, Maria Vivo, Girolama La Mantia

  • 1Department of Structural and Functional Biology, University of Naples Federico II, Naples, Italy. apollice@unina.it

FEBS Letters
|September 23, 2008
PubMed

Insights

The tumor suppressor ARF protein acts as a crucial stress sensor. This review explores how the proteasome regulates ARF and its partners, revealing a complex interaction network.

Area of Science:

  • Cellular Biology
  • Molecular Oncology
  • Protein Degradation

Background:

  • The ARF (Alternative Reading Frame) protein is a key tumor suppressor and oncogenic stress sensor in mammalian cells.
  • ARF exerts its tumor-suppressive functions by interacting with and inactivating various cellular partners.
  • Understanding ARF's regulation is critical for cancer research.

Purpose of the Study:

  • To review the role of the proteasome in regulating ARF protein turnover.
  • To elucidate the impact of proteasome-mediated regulation on ARF's interacting partners.
  • To highlight the intricate network between ARF and the proteasome.

Main Methods:

  • Literature review focusing on proteasome function and ARF interactions.
  • Analysis of studies investigating ARF protein stability and degradation pathways.
  • Synthesis of current knowledge on ARF-proteasome interplay.

Main Results:

  • The proteasome plays a significant role in controlling ARF protein levels and turnover.
  • Specific proteasome components are implicated in the regulation of ARF.
  • Proteasome activity influences the function of ARF's interacting partners.

Conclusions:

  • A complex regulatory network exists between ARF and the proteasome.
  • The proteasome is a key modulator of ARF's tumor-suppressive activity.
  • Further research into this interaction may reveal novel therapeutic strategies for cancer.

More Related Videos

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis05:43

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

Assaying Proteasomal Degradation in a Cell-free System in Plants07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Related Concept Videos

The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...