Related Experiment Video
Updated: Dec 30, 2025
07:43
Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
15.0K
Golgi organization is regulated by proteasomal degradation
Avital Eisenberg-Lerner1, Ron Benyair1, Noa Hizkiahou1
1Department of Immunology, Weizmann Institute of Science, Rehovot, Israel.
Nature Communications
|January 23, 2020
Summary
Researchers discovered that proteasomes degrade GM130 to enable Golgi dispersal under stress. This Golgi-localized proteasomal degradation offers a new therapeutic strategy for multiple myeloma by perturbing Golgi homeostasis.
Area of Science:
- Cell Biology
- Molecular Biology
- Cancer Biology
Background:
- The Golgi apparatus is vital for cellular homeostasis, and its structural integrity is linked to diseases like cancer and neurodegeneration.
- The mechanisms regulating Golgi dispersal under cellular stress and its functional consequences are not fully understood.
Purpose of the Study:
- To investigate the active regulation of Golgi apparatus dispersal under stress conditions.
- To elucidate the role of proteasomes and specific proteins in Golgi stress response and dispersal.
- To explore the therapeutic potential of targeting Golgi homeostasis in multiple myeloma.
Main Methods:
- Immunofluorescence microscopy to visualize Golgi structure and protein localization.
- Biochemical assays to study protein degradation and proteasome activity.
- Cell viability assays and in vivo studies in mouse models of multiple myeloma.
Main Results:
- 26S proteasomes associate with Golgi membranes to mediate Golgi Apparatus-Related Degradation (GARD).
- Degradation of GM130, dependent on p97/VCP and 26S proteasomes, is essential for Golgi dispersal.
- Perturbing Golgi homeostasis induces cell death in multiple myeloma cells both in vitro and in vivo.
Conclusions:
- A novel mechanism of Golgi-localized proteasomal degradation (GARD) is revealed.
- Proteostasis control is functionally linked to Golgi architecture maintenance.
- Targeting Golgi homeostasis presents a potential therapeutic strategy for multiple myeloma.
Related Concept Videos
01:49Golgi Apparatus
99.5K
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
99.5K
01:09Golgi Apparatus
20.9K
Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
20.9K
02:18The Proteasome
9.9K
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...
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...
9.9K
01:13The Proteasome
1.5K
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...
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...
1.5K
02:18The Proteasome
4.3K
4.3K
02:58Regulated Protein Degradation
8.6K
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...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.6K