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

8.9K
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...
8.9K
Regulated Protein Degradation02:58

Regulated Protein Degradation

7.5K
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...
7.5K
The Proteasome Structure01:17

The Proteasome Structure

857
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...
857
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

6.8K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
6.8K
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

12.4K
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...
12.4K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K

You might also read

Related Articles

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

Sort by
Same author

A Degron Decoy System Co-opts Pathological Seeding to Enable Clearance of Multimeric α-Synuclein.

bioRxiv : the preprint server for biology·2026
Same author

A PKA-selective inhibitor captures an open but more ordered conformation of the PKA catalytic subunit.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Correction: Discovery and optimization of tau targeted protein degraders enabled by patient induced pluripotent stem cells-derived neuronal models of tauopathy.

Frontiers in cellular neuroscience·2026
Same author

Development of PROTACs for targeted degradation of oncogenic TRK fusions.

RSC chemical biology·2026
Same author

The APEXTAC System for Ligand-Guided Proximity Labeling.

Chembiochem : a European journal of chemical biology·2025
Same author

Synthesis and Structure-Activity Relationships of CRBN-Recruiting ZBTB11 Molecular Glue Degraders.

Journal of medicinal chemistry·2025
Same journal

Decoding Viral Dark Matter: Metagenomic Prokaryotic Virus Characterization With Pharokka, Phold, and Phynteny.

Current protocols·2026
Same journal

A Novel Laboratorial Approach to Evaluate Bacterial Microleakage of Endodontic Sealers.

Current protocols·2026
Same journal

TRIAGE Toolkit: Streamlined Discovery of Regulatory Genes and Elements.

Current protocols·2026
Same journal

High-throughput Profiling of Pseudouridines in Microbiome-derived Bacterial RNA.

Current protocols·2026
Same journal

Recombinant Protein Expression in Rhodococcus species.

Current protocols·2026
Same journal

Streamlined In Vitro Transcription for Generating Self-Amplifying RNA With Modified Nucleotides.

Current protocols·2026
See all related articles

Related Experiment Video

Updated: Aug 18, 2025

High-Throughput Cellular Profiling of Targeted Protein Degradation Compounds Using HiBiT CRISPR Cell Lines
05:33

High-Throughput Cellular Profiling of Targeted Protein Degradation Compounds Using HiBiT CRISPR Cell Lines

Published on: November 9, 2020

10.0K

Targeted Protein Degradation: Design Considerations for PROTAC Development.

Nathan L Tran1, Georges A Leconte1, Fleur M Ferguson1,2

  • 1Department of Chemistry and Biochemistry, University of California, La Jolla, San Diego, California, USA.

Current Protocols
|December 5, 2022
PubMed
Summary
This summary is machine-generated.

Targeted protein degraders, like Proteolysis-targeting chimeras (PROTACs), offer a novel therapeutic strategy by harnessing the cell's natural degradation pathways. This approach enables targeting previously inaccessible proteins for degradation, expanding research and treatment possibilities.

Keywords:
PROTACcompound optimizationmedicinal chemistryproteolysis-targeting chimeratargeted protein degradation

More Related Videos

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

3.6K
Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
10:44

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

Published on: May 15, 2019

13.3K

Related Experiment Videos

Last Updated: Aug 18, 2025

High-Throughput Cellular Profiling of Targeted Protein Degradation Compounds Using HiBiT CRISPR Cell Lines
05:33

High-Throughput Cellular Profiling of Targeted Protein Degradation Compounds Using HiBiT CRISPR Cell Lines

Published on: November 9, 2020

10.0K
Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

3.6K
Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
10:44

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

Published on: May 15, 2019

13.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Targeted protein degradation is a rapidly growing field in therapeutic strategy and biomedical research.
  • Targeted protein degraders can access previously undruggable targets due to sub-stoichiometric requirements and lack of need for high binding affinity.
  • Proteolysis-targeting chimeras (PROTACs) are a key class of targeted protein degraders.

Purpose of the Study:

  • To provide resources and methodologies for developing PROTAC degraders.
  • To guide researchers new to the field of targeted protein degradation.
  • To highlight the potential of PROTACs in biomedical research and therapeutics.

Main Methods:

  • Development of heterobifunctional molecules (PROTACs) that bridge target proteins and E3 ligase complexes.
  • Rational design and systematic optimization strategies for PROTACs.
  • Leveraging the modular nature of PROTACs for tailored applications.

Main Results:

  • PROTACs effectively recruit target proteins to E3 ligase complexes, inducing degradation.
  • The modular design facilitates the creation of diverse PROTAC molecules.
  • Methodologies for PROTAC development are presented for broader accessibility.

Conclusions:

  • PROTACs represent a powerful and versatile tool for targeted protein degradation.
  • The development of PROTACs offers significant potential for novel therapeutic strategies.
  • This work provides a foundational guide for researchers entering the PROTAC field.