Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
Export of Misfolded Proteins out of the ER01:32

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...
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...

You might also read

Related Articles

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

Sort by
Same author

Early-onset neuroinflammation drives neurodegeneration caused by lysosomal PI(3,5)P<sub>2</sub> insufficiency.

Neurobiology of disease·2026
Same author

The autophagic and non-autophagic functions of the <i>S. cerevisiae</i> PROPPIN Hsv2.

Autophagy·2026
Same author

Formation and function of a novel Atg21-retromer complex in <i>S. cerevisiae</i>.

Autophagy·2026
Same author

Microautophagy: current understanding of its molecular mechanisms and functions.

Autophagy reports·2026
Same author

Rab24 protein levels show dynamic changes in mouse tissues and human cancers.

Cell and tissue research·2026
Same author

The RAB27A effector SYTL5 regulates mitophagy and mitochondrial metabolism.

eLife·2025

Related Experiment Video

Updated: Jun 6, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

Cheating on ubiquitin with Atg8.

Roswitha Krick1, Sebastian Bremer, Evelyn Welter

  • 1Department Biochemistry II, Georg-August University, Goettingen, Germany.

Autophagy
|December 15, 2010
PubMed
Summary

Macroautophagy uses the ubiquitin-like protein Atg8 for autophagosome formation. Researchers investigated the involvement of yeast homologues Cdc48 and Shp1 in this essential cellular process.

Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Macroautophagy is a cellular process for degrading waste, involving the formation of double-membraned autophagosomes.
  • Over 30 autophagy-related (ATG) genes are known, but the precise mechanisms of autophagosome biogenesis, particularly membrane fusion, remain unclear.
  • The ubiquitin-like protein Atg8 is implicated in autophagosome elongation, yet its role in membrane fusion is not fully understood.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying autophagosome biogenesis.
  • To explore the potential role of the AAA (+) ATPase homologues Cdc48 and Shp1 in macroautophagy, given their involvement in similar membrane fusion events in other cellular processes.

Main Methods:

  • Analysis of the involvement of yeast homologues Cdc48 and Shp1 in macroautophagy.

More Related Videos

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Related Experiment Videos

Last Updated: Jun 6, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

  • Comparison of autophagosome formation with topologically similar processes like nuclear envelope growth and Golgi fragment fusion.
  • Main Results:

    • The study analyzed the involvement of Cdc48 and Shp1 in macroautophagy.
    • The research explored the functional similarity between autophagosome formation and other membrane fusion events.

    Conclusions:

    • The findings contribute to understanding the molecular machinery of autophagosome biogenesis.
    • Further research is needed to elucidate the specific roles of Cdc48 and Shp1 in macroautophagy and membrane fusion.