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...
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.
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.
The Central Dogma01:25

The Central Dogma

Overview

You might also read

Related Articles

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

Sort by
Same author

Systemic degradation of repressive transcription factors gates gene expression and cell fate specification.

bioRxiv : the preprint server for biology·2026
Same author

Localized heme sensing through a ternary molecular glue.

bioRxiv : the preprint server for biology·2026
Same author

Ubiquitination of glycogen and metabolites in cells and tissues.

Nature·2026
Same author

GID/CTLH E3 ligase complex control cell fate programs for sexual development of Plasmodium falciparum.

Nature communications·2026
Same author

Global analysis of cancer cell responses to USP9X inhibition.

The EMBO journal·2026
Same author

The E3-ome gene-centric compendium reveals the human E3 ligase landscape.

Cell·2026
Same journal

Lactate as a Chemical Modification on Proteins and Metabolites.

Annual review of biochemistry·2026
Same journal

Nucleocytoplasmic Transport.

Annual review of biochemistry·2026
Same journal

Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles.

Annual review of biochemistry·2026
Same journal

Shaping of the Infant Gut Microbiome by Milk Oligosaccharides.

Annual review of biochemistry·2026
Same journal

Proteostasis Deregulation by Metabolism Drives the Hallmarks of Cancer.

Annual review of biochemistry·2026
Same journal

JoAnne Stubbe's Radical Path: A Story of Passion, Curiosity, and Persistence.

Annual review of biochemistry·2026
See all related articles

Related Experiment Video

Updated: May 23, 2026

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

The ubiquitin code.

David Komander1, Michael Rape

  • 1Division of Protein and Nucleic Acid Chemistry, Medical Research Council Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom. dk@mrc-lmb.cam.ac.uk

Annual Review of Biochemistry
|April 25, 2012
PubMed
Summary
This summary is machine-generated.

Ubiquitylation, a key cellular process, involves attaching ubiquitin to proteins, forming chains that act like a code. This ubiquitin code dictates distinct cellular outcomes based on its structure and assembly.

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

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Related Experiment Videos

Last Updated: May 23, 2026

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

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Area of Science:

  • Cellular biology
  • Biochemistry
  • Molecular biology

Background:

  • Posttranslational modifications regulate cellular functions.
  • Ubiquitylation is a critical modification controlling numerous cellular processes.
  • Ubiquitin can be conjugated as single units or polymeric chains.

Purpose of the Study:

  • To discuss the structure, assembly, and function of the ubiquitin code.
  • To highlight the regulatory role of ubiquitin modifications in cellular processes.

Main Methods:

  • Structural analysis of ubiquitin chains.
  • Biochemical assays for ubiquitin chain assembly.
  • Functional studies on the impact of different ubiquitin codes.

Main Results:

  • Ubiquitin modifications adopt distinct conformations.
  • Polymeric ubiquitin chains are formed via specific isopeptide bonds.
  • Different ubiquitin chain structures lead to diverse cellular outcomes.

Conclusions:

  • The ubiquitin code is a complex regulatory system.
  • Understanding ubiquitin structure and assembly is crucial for deciphering cellular signaling.
  • Ubiquitylation plays a central role in virtually all cellular activities.