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

Understanding cullin-RING E3 biology through proteomics-based substrate identification.

J Wade Harper1, Meng-Kwang Marcus Tan

  • 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. wade_harper@hms.harvard.edu

Molecular & Cellular Proteomics : MCP
|September 11, 2012
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

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026
Same author

A human lysosomal storage disorder toolkit for decoding proteome landscapes in cortical-like and dopaminergic-like induced neurons.

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

Structural basis for regulation of the proteasome 20S core particle by the Parkinsonism-associated proteins FBXO7 and PI31.

bioRxiv : the preprint server for biology·2026
Same author

Membrane bridges and nanodomain partitioning govern membrane protein targeting to lipid droplets.

Nature cell biology·2026
Same author

Components of an ESCRT-independent nuclear envelope assembly pathway.

bioRxiv : the preprint server for biology·2026
Same author

Machine learning enables efficient and effective affinity maturation of nanobodies.

bioRxiv : the preprint server for biology·2026

Identifying protein targets of ubiquitin ligases is crucial for understanding cellular processes. This review details proteomic methods for discovering these targets, focusing on the cullin-RING E3 ligase family, aiding future research in the ubiquitin-proteasome pathway.

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • The ubiquitin-proteasome pathway regulates critical cellular functions, including development and biochemical processes.
  • Ubiquitin ligases confer specificity to protein ubiquitylation, a key mechanism in protein turnover.
  • The human genome encodes over 600 ubiquitin ligases, many of which require further investigation.

Purpose of the Study:

  • To review and compare proteomic technologies for identifying ubiquitin ligase substrates.
  • To highlight methods applicable to the cullin-RING E3 class of ubiquitin ligases.
  • To discuss the impact of these technologies on the ubiquitin-proteasome field.

Main Methods:

  • Proteomic technologies for substrate identification are described.

Related Experiment Videos

  • Specific focus on methods for cullin-RING E3 ubiquitin ligases and their F-box protein adaptors.
  • Comparison of proteomic approaches with available genetic methods.

    • Main Results:

    • The review synthesizes current proteomic strategies for ubiquitin ligase target discovery.
    • It provides a comparative analysis of different methodologies.
    • It emphasizes the importance of F-box proteins in substrate recognition for cullin-RING E3 ligases.

    Conclusions:

    • Advancements in proteomic technologies are essential for elucidating the functions of numerous uncharacterized ubiquitin ligases.
    • These methods facilitate the identification of specific ubiquitin ligase targets, advancing the understanding of the ubiquitin-proteasome system.
    • Continued development of these techniques will significantly impact the field of protein ubiquitylation and turnover.