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Related Concept Videos

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...
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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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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Changes in proteasome structure and function caused by HAMLET in tumor cells.

Lotta Gustafsson1, Sonja Aits, Patrik Onnerfjord

  • 1Department of Microbiology, Institute of Laboratory Medicine, Lund University, Lund, Sweden.

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The protein complex HAMLET targets proteasomes, resisting degradation and inhibiting their activity. This interaction perturbs proteasome structure, potentially contributing to cell death in tumor cells.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Proteasomes degrade unfolded proteins, preventing cell death.
  • HAMLET, a protein-lipid complex, induces cell death in tumor cells.

Purpose of the Study:

  • To investigate the interaction between HAMLET and proteasomes.
  • To understand the effect of HAMLET on proteasome function and structure.

Main Methods:

  • In vitro binding assays with isolated 20S proteasomes.
  • Confocal microscopy and co-immunoprecipitation in tumor cells.
  • Assays for proteasome activity and structural analysis.

Main Results:

  • HAMLET directly binds to 20S proteasomes in vitro and in tumor cells.
  • HAMLET resists proteasomal degradation and inhibits proteasome activity.
  • HAMLET binding alters proteasome structure, affecting catalytic and structural subunits.

Conclusions:

  • HAMLET targets 20S proteasomes, resisting degradation and inhibiting activity.
  • HAMLET binding perturbs proteasome structure, potentially mediating its cytotoxic effects.
  • HAMLET-induced proteasome dysfunction may contribute to tumor cell death.