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Related Concept Videos

The Proteasome01:13

The Proteasome

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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...
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The Proteasome02:18

The Proteasome

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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.
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The Proteasome02:18

The Proteasome

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Regulated Protein Degradation02:58

Regulated Protein Degradation

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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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Regulated Protein Degradation02:58

Regulated Protein Degradation

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The Proteasome Structure01:17

The Proteasome Structure

2.1K
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...
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Related Experiment Video

Updated: Mar 17, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
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An evolutionarily conserved pathway controls proteasome homeostasis.

Adrien Rousseau, Anne Bertolotti

    Nature
    |July 28, 2016
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    Summary
    This summary is machine-generated.

    A conserved signaling pathway regulates proteasome levels. Inhibiting TORC1 activates Mpk1, increasing proteasome components for cell survival under stress. This pathway is conserved in mammals.

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    Area of Science:

    • Cellular biology
    • Molecular biology
    • Biochemistry

    Background:

    • The proteasome is crucial for protein degradation, yet mechanisms maintaining its abundance (proteasome homeostasis) are not fully understood.
    • Cellular proteasome levels must be tightly regulated to meet cellular demands for protein turnover.

    Purpose of the Study:

    • To elucidate the signaling pathways governing proteasome homeostasis.
    • To identify key regulators controlling proteasome subunit and assembly chaperone production.

    Main Methods:

    • Yeast genetics and molecular biology techniques were employed to study the role of TORC1 and Mpk1.
    • Mammalian cell culture and molecular analyses were used to assess evolutionary conservation.

    Main Results:

    • Inhibition of TORC1 (target of rapamycin complex 1) in yeast induced the expression of 19S regulatory particle assembly-chaperones (RACs) and proteasome subunits.
    • Downstream of TORC1, the Mpk1 (mitogen-activated protein kinase) pathway was activated, increasing RACs and proteasome subunits, thereby maintaining proteasomal degradation and cell viability under stress.
    • The pathway involving mTOR (mammalian TOR) and ERK5 (extracellular signal-regulated kinase 5) was found to be conserved in mammals, controlling RAC levels and proteasome abundance.

    Conclusions:

    • A conserved signaling pathway, involving TORC1/mTOR and Mpk1/ERK5, rapidly adjusts proteasome abundance in response to cellular needs and stress.
    • This adaptive response is vital for maintaining proteasomal degradation and cell viability.
    • Targeting this pathway presents a potential therapeutic strategy for diseases characterized by impaired proteasomal degradation.