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Related Concept Videos

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...
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...
B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...
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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Related Experiment Video

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In Vitro Differentiation Model of Human Normal Memory B Cells to Long-lived Plasma Cells
10:26

In Vitro Differentiation Model of Human Normal Memory B Cells to Long-lived Plasma Cells

Published on: January 20, 2019

The proteasome in terminal plasma cell differentiation.

Simone Cenci1

  • 1Division of Genetics and Cell Biology, DiBiT, San Raffaele Scientific Institute, and Università Vita-Salute San Raffaele, Milano, Italy. cenci.simone@hsr.it

Seminars in Hematology
|June 26, 2012
PubMed
Summary

During B-cell activation, proteasome capacity collapses, leading to proteotoxic stress and vulnerability to proteasome inhibition. This proteostenosis has implications for antibody production and autoimmune diseases.

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Area of Science:

  • Cell Biology
  • Immunology
  • Molecular Biology

Background:

  • Eukaryotic cells regulate their proteome to adapt and differentiate.
  • Protein degradation is crucial for maintaining protein homeostasis.
  • Activated B lymphocytes undergo significant changes for antibody secretion.

Purpose of the Study:

  • To investigate the regulation of protein homeostasis during B-cell activation.
  • To understand the implications of proteasome capacity collapse in antibody-secreting cells.
  • To explore the role of proteotoxicity in B-cell biology and autoimmune diseases.

Main Methods:

  • Analysis of proteasome capacity during B-cell activation.
  • Assessment of proteotoxic stress markers in antibody-secreting cells.
  • Investigation of cellular responses to proteasome inhibition.

Main Results:

  • Proteasome capacity significantly decreases during B-cell metamorphosis.
  • Antibody-secreting cells exhibit symptoms of proteotoxic stress.
  • These cells become highly vulnerable to proteasome inhibitors.

Conclusions:

  • Proteostenosis naturally occurs after B-cell activation, impacting protein homeostasis.
  • This phenomenon offers a model for studying integrated protein regulation.
  • It also presents a molecular mechanism that limits antibody responses, potentially useful in autoimmune disease therapy.