Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

Regulated Protein Degradation

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...

Regulated Protein Degradation

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...

Nonsense-mediated mRNA Decay

Nonsense-mediated mRNA Decay

The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...

Nuclear Export of mRNA

Nuclear Export of mRNA

Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...

Proteins: From Genes to Degradation

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick. Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.

The Journal of biological chemistry·2019

Same author

Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.

Proceedings of the National Academy of Sciences of the United States of America·2017

Same author

Ricin trafficking in cells.

Toxins·2015

Same author

The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain.

The Biochemical journal·2013

Same author

Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p.

PloS one·2012

Same author

Ricin trafficking in plant and mammalian cells.

Toxins·2011

Search research articles

Related Experiment Video

Updated: Jul 18, 2026

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Published on: November 6, 2014

Quality control: linking retrotranslocation and degradation.

Colin J Stirling¹, J Michael Lord

¹Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.

Current Biology : CB

|December 19, 2006

Summary

Misfolded proteins are moved out of the ER by the p97 AAA ATPase for degradation. The protein ataxin-3 may regulate how these proteins reach the proteasome after dislocation.

Area of Science:

Cellular Biology
Protein Degradation Pathways

Background:

Misfolded proteins accumulate in the endoplasmic reticulum (ER) and must be removed.
The p97 AAA ATPase enzyme complex is essential for retro-translocation of misfolded proteins from the ER to the cytosol.
Degradation of these proteins by the cytosolic proteasome is a critical cellular quality control mechanism.

Purpose of the Study:

To investigate the mechanism by which proteins dislocated by p97 AAA ATPase are delivered to the proteasome.
To explore the potential regulatory role of ataxin-3 in this protein degradation pathway.

Main Methods:

Utilizing biochemical assays to study protein-p97 interactions.
Employing cellular imaging techniques to track protein trafficking.
Investigating the impact of ataxin-3 on protein dislocation and degradation.

More Related Videos

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Related Experiment Videos

Last Updated: Jul 18, 2026

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Published on: November 6, 2014

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Main Results:

Evidence suggests that ataxin-3 interacts with p97.
Ataxin-3 appears to influence the efficiency of protein delivery to the proteasome post-dislocation.
The precise role of ataxin-3 in regulating the p97-mediated degradation pathway is being elucidated.

Conclusions:

The protein ataxin-3 plays a significant role in the clearance of misfolded proteins.
Understanding ataxin-3's function provides insights into ER-associated degradation and cellular proteostasis.
Further research is needed to fully characterize the ataxin-3 regulatory mechanism in p97-mediated protein degradation.