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

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...
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...
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 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

A unified catalytic mechanism in bifunctional DNA glycosylases with an evolutionarily conserved aspartate-lysine dyad.

Nature communications·2026
Same author

Inhibition of ADSS2-mediated de novo AMP biosynthesis re-sensitizes acute myeloid leukemia to BH3 mimetics.

Nature cancer·2026
Same author

PARG Governs a PARylation-Ubiquitination Toggle that Stabilizes RAD51AP1 to Drive Homologous Recombination-Mediated Chemoresistance.

Cancer research·2026
Same author

Targeting the METTL1/m7G axis as a therapeutic strategy in myeloid leukemia.

Blood·2026
Same author

Orchestrated metal ion repositioning defines the dynamic catalytic strategy of the essential DNA repair nuclease APE1.

bioRxiv : the preprint server for biology·2026
Same author

Characteristics and Clinical Outcomes of BRCA Germline Mutation Carriers with Advanced Breast Cancer Treated with PARP (Poly ADP-Ribose Polymerase) Inhibitors: A Single-Institution Experience.

Cancers·2026

Related Experiment Video

Updated: Jul 6, 2026

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
09:40

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

A SIM-ultaneous role for SUMO and ubiquitin.

J Jefferson P Perry1, John A Tainer, Michael N Boddy

  • 1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Trends in Biochemical Sciences
|April 12, 2008
PubMed
Summary

Small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs) link sumoylation and ubiquitylation, regulating protein levels. Loss of STUbLs causes genomic instability, highlighting their crucial cellular roles.

More Related Videos

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
08:29

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

Published on: November 1, 2019

Related Experiment Videos

Last Updated: Jul 6, 2026

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
09:40

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
08:29

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

Published on: November 1, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Ubiquitin and ubiquitin-like proteins (Ubls) share structural similarities and cellular functions.
  • Small ubiquitin-related modifier (SUMO) and ubiquitin are often viewed as distinct with opposing roles.
  • Small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs) represent a novel protein family connecting sumoylation and ubiquitylation pathways.

Purpose of the Study:

  • To investigate the function of STUbLs in cellular processes.
  • To understand how STUbLs recognize their targets.
  • To explore the role of STUbLs in maintaining genomic stability.

Main Methods:

  • Identification and characterization of STUbLs.
  • Analysis of STUbL-substrate interactions using SUMO-interaction motifs (SIMs).
  • Assessment of cellular phenotypes in STUbL-deficient cells, including genomic instability and stress response.

Main Results:

  • STUbLs utilize SIMs to bind sumoylated targets, directly linking sumoylation and ubiquitylation.
  • STUbLs act as global regulators of protein sumoylation.
  • Absence of STUbLs leads to genomic instability and increased sensitivity to genotoxic stress.

Conclusions:

  • STUbLs are critical regulators of protein modification pathways.
  • STUbLs play a vital role in maintaining genome integrity.
  • Dysfunction of STUbLs, like RNF4, is associated with diseases such as cancer.