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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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
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...

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Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein
10:25

Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein

Published on: November 10, 2012

Physiological levels of ATP negatively regulate proteasome function.

Hongbiao Huang1, Xiaoyan Zhang, Shujue Li

  • 1Protein Modification and Degradation Lab, Department of Pathophysiology, Guangzhou Medical College, Guangzhou, Guangdong 510182, China.

Cell Research
|September 1, 2010
PubMed
Summary
This summary is machine-generated.

Adenosine triphosphate (ATP) bidirectionally regulates the 26S proteasome, impacting protein degradation. Physiological ATP levels can inhibit proteasome activity, allowing cells to adapt to stress by increasing protein degradation when ATP is reduced.

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Assaying Proteasomal Degradation in a Cell-free System in Plants
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Monitoring of Ubiquitin-proteasome Activity in Living Cells Using a Degron (dgn)-destabilized Green Fluorescent Protein (GFP)-based Reporter Protein
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • The ubiquitin-proteasome system (UPS) is crucial for intracellular protein degradation.
  • Proteasome function is dependent on adenosine triphosphate (ATP).
  • In vitro studies show optimal proteasome activation at ~100 microM ATP, yet physiological millimolar ATP levels can inhibit activity.

Purpose of the Study:

  • To investigate the hypothesis that intracellular ATP bidirectionally regulates 26S proteasome function.
  • To elucidate the role of physiological ATP concentrations in controlling proteasome activity within cells.

Main Methods:

  • In vitro assays to assess ATP's effect on 26S proteasome chymotrypsin-like activity.
  • Manipulation of intracellular ATP levels in cultured cells.
  • Evaluation of proteasome-specific substrate levels following ATP manipulation.
  • Assessment of cell death induction by proteasome inhibition under varying intracellular ATP conditions.

Main Results:

  • ATP demonstrated bidirectional regulation of 26S proteasome activity in vitro, with optimal stimulation between 50-100 microM.
  • Changes in intracellular ATP levels resulted in corresponding bidirectional shifts in proteasome substrate levels in cells.
  • Increased intracellular ATP enhanced, while decreased ATP attenuated, the cell death response to proteasome inhibition.

Conclusions:

  • Endogenous ATP within the physiological concentration range negatively impacts proteasome activity.
  • This regulation allows cells to rapidly upregulate proteasome activity during stress conditions characterized by ATP reduction.
  • Physiological ATP levels act as a dynamic modulator of proteasome-mediated protein degradation.