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 Proteasome02:18

The Proteasome

10.3K
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...
10.3K
The Proteasome01:13

The Proteasome

1.7K
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...
1.7K
The Proteasome02:18

The Proteasome

4.6K
4.6K
Regulated Protein Degradation02:58

Regulated Protein Degradation

8.9K
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...
8.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.6K
The Proteasome Structure01:17

The Proteasome Structure

1.7K
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...
1.7K

You might also read

Related Articles

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

Sort by
Same author

The selective degradation of PDE4B shortform, using a PROTAC, leads to inhibition of several hallmarks of cancer in HCT116 cells.

British journal of pharmacology·2026
Same author

KTX207-mediated PDE4D degradation disrupts tumour cell migration, invasion, and angiogenic potential.

Cell communication and signaling : CCS·2026
Same author

Cardiopulmonary Consequences of Scoliosis and the Clinical Implications of VO<sub>2</sub>max: A Systematic Review.

Journal of the Pediatric Orthopaedic Society of North America·2026
Same author

Matrix structure and microenvironment dynamics correlate with chemotherapy response in ovarian cancer.

iScience·2026
Same author

3D pentaculture model unveils malignant cell-driven macrophage polarization in high-grade serous ovarian cancer.

Nature communications·2026
Same author

Rheumatoid arthritis and interstitial lung disease: the role of comorbidities-a retrospective analysis of two RA inception cohorts in the UK.

Rheumatology (Oxford, England)·2026

Related Experiment Video

Updated: Feb 6, 2026

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

7.2K

RAB40C regulates RACK1 stability via the ubiquitin-proteasome system.

Jon P Day1,1, Ellanor Whiteley1,1, Michael Freeley2,2

  • 1Institute of Cardiovascular & Medical Sciences, University of Glasgow, Glasgow G12 8QQ, UK.

Future Science OA
|August 17, 2018
PubMed
Summary

Researchers identified RAB40C as the E3 ligase controlling RACK1 protein levels. This discovery is vital for understanding cancer cell growth and T cell migration, offering new therapeutic strategies.

Keywords:
RAB40CRACK1ubiquitin–proteasome system

More Related Videos

siRNA Screening to Identify Ubiquitin and Ubiquitin-like System Regulators of Biological Pathways in Cultured Mammalian Cells
10:43

siRNA Screening to Identify Ubiquitin and Ubiquitin-like System Regulators of Biological Pathways in Cultured Mammalian Cells

Published on: May 24, 2014

11.8K
Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

4.1K

Related Experiment Videos

Last Updated: Feb 6, 2026

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

7.2K
siRNA Screening to Identify Ubiquitin and Ubiquitin-like System Regulators of Biological Pathways in Cultured Mammalian Cells
10:43

siRNA Screening to Identify Ubiquitin and Ubiquitin-like System Regulators of Biological Pathways in Cultured Mammalian Cells

Published on: May 24, 2014

11.8K
Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

4.1K

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Receptor for Activated C Kinase 1 (RACK1) is a versatile scaffolding protein involved in numerous signaling pathways.
  • RACK1's role as a signaling hub necessitates precise regulation for cellular homeostasis.
  • Understanding RACK1 turnover mechanisms is critical for cellular function.

Purpose of the Study:

  • To elucidate the mechanisms governing RACK1 protein degradation.
  • To identify the specific ubiquitin E3 ligase responsible for RACK1 ubiquitination.
  • To investigate the role of RACK1 regulation in cancer and immune cell function.

Main Methods:

  • siRNA screening to identify key proteins involved in RACK1 regulation.
  • Ubiquitination assays to confirm the E3 ligase activity.
  • Cell-based assays to assess the impact on cancer cell growth and T cell migration.

Main Results:

  • RAB40C was identified as the ubiquitin E3 ligase that targets RACK1 for degradation.
  • RAB40C-mediated regulation of RACK1 levels is essential for cancer cell proliferation.
  • RAB40C controls RACK1 levels, impacting T cell migration.

Conclusions:

  • RACK1 degradation is mediated by the ubiquitin proteasome system, with RAB40C as the E3 ligase.
  • Targeting RACK1 levels via RAB40C presents a potential therapeutic strategy.
  • Further exploration of RACK1 modulation could reveal novel insights into cellular signaling and disease.