Related Experiment Video

Updated: Aug 28, 2025

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
08:44

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models

Published on: November 11, 2014

8.3K

J Proteins Counteract Amyloid Propagation and Toxicity in Yeast

Daniel C Masison1, Michael Reidy1, Jyotsna Kumar2

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Biology
|September 23, 2022
PubMed

Insights

Misfolded proteins forming amyloids cause diseases like Alzheimer's. J-domain proteins (JDPs) help counteract amyloid toxicity in yeast by regulating protein quality control, often with Hsp70 chaperones.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Amyloid protein accumulation is linked to neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's.
  • Yeast models are valuable for studying amyloid toxicity and cellular responses to misfolded proteins.

Purpose of the Study:

  • To explore protein quality control factors that counteract amyloid propagation and toxicity.
  • To emphasize the role of J-domain proteins (JDPs) in managing amyloidogenic proteins.

Main Methods:

  • Utilizing yeast as a model system to express human amyloid-forming proteins.
  • Investigating the function of J-domain proteins (JDPs) and their interaction with Hsp70 chaperones.

Main Results:

  • J-domain proteins (JDPs) are key regulators of Hsp70 chaperones and are abundant in yeast.
  • JDPs demonstrate anti-amyloid effects, either directly or through Hsp70 interaction.

Conclusions:

  • Protein quality control mechanisms, particularly JDPs, are crucial for mitigating amyloid toxicity.
  • Understanding JDPs and Hsp70 interactions offers potential therapeutic targets for amyloid-related diseases.
Keywords:
J proteinsamyloidpolyglutamineprions

More Related Videos

High-throughput Yeast Plasmid Overexpression Screen08:57

High-throughput Yeast Plasmid Overexpression Screen

Published on: July 27, 2011

16.5K
A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model08:24

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

2.3K

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.7K
Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
14.8K