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

Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
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...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

You might also read

Related Articles

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

Sort by
Same author

The role of epithelial membrane-associated mucin 4 in ocular surface health and corneal wound healing.

Frontiers in medicine·2026
Same author

A novel lipophilic amiloride derivative efficiently kills chemoresistant breast cancer cells.

Scientific reports·2024
Same author

Genetic Screen in a Preclinical Model of Sarcoma Development Defines Drivers and Therapeutic Vulnerabilities.

Clinical cancer research : an official journal of the American Association for Cancer Research·2024
Same author

A complex of Wnt/planar cell polarity signaling components Vangl1 and Fzd7 drives glioblastoma multiforme malignant properties.

Cancer letters·2023
Same author

Structure-Activity Relationship Study Identifies a Novel Lipophilic Amiloride Derivative that Efficiently Kills Chemoresistant Breast Cancer Cells.

bioRxiv : the preprint server for biology·2023
Same author

Vangl-dependent Wnt/planar cell polarity signaling mediates collective breast carcinoma motility and distant metastasis.

Breast cancer research : BCR·2023

Related Experiment Video

Updated: Jun 8, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

E3 ubiquitin ligases in ErbB receptor quantity control.

Kermit L Carraway1

  • 1UC Davis Cancer Center, Sacramento, CA 95817, USA. klcarraway@ucdavis.edu

Seminars in Cell & Developmental Biology
|September 28, 2010
PubMed
Summary

Cellular control of ErbB receptor levels is crucial for development and preventing cancer. Protein degradation pathways, involving E3 ubiquitin ligases, are key to regulating ErbB receptor quantity and suppressing tumor growth.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • ErbB receptor tyrosine kinases are vital for tissue development and homeostasis.
  • Aberrant ErbB signaling, either insufficient or excessive, can lead to developmental issues or cancer.
  • Mechanisms controlling ErbB receptor levels, termed "ErbB receptor quantity control," are critical for maintaining cellular balance.

Purpose of the Study:

  • To review the role of post-transcriptional regulation, specifically protein degradation, in ErbB receptor quantity control.
  • To discuss the involvement of specific E3 ubiquitin ligases in the degradation of ErbB receptors.
  • To propose a hypothesis regarding the function of protein degradation in preventing ErbB receptor overexpression and its link to cancer.

Main Methods:

More Related Videos

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
10:27

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Published on: December 5, 2019

Related Experiment Videos

Last Updated: Jun 8, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
10:27

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Published on: December 5, 2019

  • Literature review focusing on post-transcriptional regulation of ErbB receptors.
  • Discussion of specific E3 ubiquitin ligases and their targets within the ErbB family.
  • Analysis of the implications of impaired ErbB quantity control in tumorigenesis.

    • Main Results:

    • Post-transcriptional mechanisms, particularly protein degradation, are significant in ErbB receptor quantity control.
    • E3 ubiquitin ligases such as Nrdp1, Nedd4 family ligases, and CHIP mediate the degradation of ErbB3, ErbB4, and ErbB2, respectively.
    • These degradation pathways are essential for suppressing excessive ErbB receptor levels in normal cells.

    Conclusions:

    • Protein degradation-based ErbB quantity control is a fundamental mechanism for maintaining normal cellular function.
    • Dysregulation or loss of these degradation pathways can contribute to the development and progression of ErbB-dependent cancers.
    • Targeting these degradation mechanisms may offer therapeutic strategies for ErbB-driven tumors.