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Related Concept Videos

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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Subcellular Fractionation01:32

Subcellular Fractionation

The homogenate obtained after cell lysis contains various membrane-bound organelles that can be further separated into pure fractions by subcellular fractionation. These isolates are used to study specific cellular components, analyze localized protein activity, and are even employed in diagnostics. Fractionation is typically achieved using centrifugation methods, the most common being density-gradient and differential centrifugation.
Differential Centrifugation
Differential centrifugation is...
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 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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: May 16, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Global subcellular characterization of protein degradation using quantitative proteomics.

Mark Larance1, Yasmeen Ahmad, Kathryn J Kirkwood

  • 1Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dow St, Dundee, United Kingdom.

Molecular & Cellular Proteomics : MCP
|December 18, 2012
PubMed
Summary

This study maps protein degradation across cellular compartments in U2OS cells using mass spectrometry. It reveals compartment-specific degradation patterns and a feedback loop involving the unfolded protein response.

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Last Updated: May 16, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
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Published on: March 26, 2014

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation
07:47

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Published on: November 6, 2014

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Area of Science:

  • Cell Biology
  • Proteomics
  • Biochemistry

Background:

  • Protein degradation is crucial for regulating cellular processes, including the cell cycle.
  • Understanding the spatial regulation of protein degradation is essential for comprehending cellular control mechanisms.

Purpose of the Study:

  • To comprehensively analyze the spatial control of protein degradation in U2OS osteosarcoma cells.
  • To identify compartment-specific protein degradation dynamics and regulatory mechanisms.

Main Methods:

  • Utilized SILAC-based quantitative mass spectrometry combined with drug treatment.
  • Employed subcellular and protein fractionation to analyze nuclear, cytosolic, membrane, and cytoskeletal compartments.
  • Analyzed over 74,000 peptides, representing approximately 5000 proteins.

Main Results:

  • Identified rapidly degraded proteasome targets, including PRR11.
  • Discovered a feedback mechanism leading to translation inhibition upon proteasome blockade, mediated by the unfolded protein response.
  • Revealed compartment-specific protein degradation differences not apparent in whole-cell lysate analyses.

Conclusions:

  • Protein degradation is spatially regulated within cells, with distinct dynamics across different compartments.
  • Proteasome inhibition triggers a feedback response involving the unfolded protein response and translation inhibition.
  • The Encyclopedia of Proteome Dynamics provides a valuable resource for exploring protein stability and subcellular distribution.