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 Experiment Videos

Ubiquitin ligation without a ligase.

Mark Hochstrasser1

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu

Developmental Cell
|July 5, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Small-molecule inhibition of the <i>Orientia tsutsugamushi</i> deubiquitylating enzyme OtDUB impairs bacterial reproduction.

bioRxiv : the preprint server for biology·2026
Same author

Sumoylation of cyclin and its therapeutic potential for cancer.

Animal cells and systems·2025
Same author

Deubiquitylases and nucleases in bacterial symbiont-induced cytoplasmic incompatibility.

Biochemical Society transactions·2025
Same author

Use of a High-Affinity Ubiquitin-Binding Domain to Detect and Purify Ubiquitinated Substrates and Their Interacting Proteins.

Bio-protocol·2025
Same author

AMPK alters proteasome phosphorylation status and prevents persistent proteasome condensates.

Genetics·2025
Same author

AMPK alters proteasome phosphorylation status and prevents persistent proteasome condensates.

bioRxiv : the preprint server for biology·2025

Researchers discovered a new way to attach ubiquitin to proteins without using E3 enzymes, similar to how SUMOylation works. This finding challenges the traditional view of ubiquitination pathways.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Ubiquitination is a crucial post-translational modification regulating numerous cellular processes.
  • Traditionally, ubiquitination involves a cascade of E1, E2, and E3 enzymes, with E3 ligases conferring substrate specificity.
  • The precise mechanisms governing protein ubiquitination are still being elucidated.

Purpose of the Study:

  • To investigate novel pathways of protein ubiquitination.
  • To explore mechanisms of monoubiquitination independent of E3 ubiquitin ligases.
  • To compare these novel mechanisms with those of SUMOylation.

Main Methods:

  • Biochemical assays to study enzyme activity.
  • In vitro reconstitution of ubiquitination reactions.

Related Experiment Videos

  • Analysis of protein modification patterns.

    • Main Results:

    • A novel E3-independent pathway for monoubiquitination was identified.
    • This mechanism shares similarities with the SUMOylation process.
    • Specific proteins were shown to undergo monoubiquitination via this alternative route.

    Conclusions:

    • The traditional model of ubiquitination requiring E3 ligases is not universally applicable.
    • E3-independent ubiquitination represents a distinct regulatory mechanism.
    • Understanding this pathway offers new insights into protein regulation and potential therapeutic targets.