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

The Doc1 subunit is a processivity factor for the anaphase-promoting complex.

Christopher W Carroll1, David O Morgan

  • 1Department of Physiology, University of California, San Francisco, CA 94143-0444, USA.

Nature Cell Biology
|October 29, 2002
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

Intramolecular loops control SARS-CoV-2 nucleocapsid protein self-association and nucleic acid binding dependent on phosphorylation.

bioRxiv : the preprint server for biology·2026
Same author

Substrate recognition by human separase.

Science advances·2025
Same author

Cohesin-mediated stabilization of the CCAN complex at kinetochores in mitosis.

Current biology : CB·2025
Same author

Phosphorylation by Aurora kinase A facilitates cortical-cytoplasmic dynamics of Par-3 in asymmetric division of radial glia progenitors.

Science advances·2025
Same author

Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.

Nature communications·2025
Same author

SARS-CoV-2 evolution balances conflicting roles of N protein phosphorylation.

PLoS pathogens·2024
Same journal

Learning from stem cell-based embryo models.

Nature cell biology·2026
Same journal

Why the temporal dimension matters in cellular signalling.

Nature cell biology·2026
Same journal

Transcription factor condensates as storage.

Nature cell biology·2026
Same journal

Author Correction: Spatial regulation of VEGF receptor endocytosis in angiogenesis.

Nature cell biology·2026
Same journal

Mitochondria-endoplasmic reticulum contact sites as hubs where mitochondria acquire iron.

Nature cell biology·2026
Same journal

Cis and trans regulatory mechanisms of extrachromosomal DNA segregation.

Nature cell biology·2026
See all related articles

The anaphase-promoting complex (APC) drives cell cycle progression by ubiquitinating proteins. The Doc1 subunit is crucial for APC

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Ubiquitin-mediated proteolysis is vital for mitotic exit.
  • The anaphase-promoting complex (APC) catalyzes the final ubiquitination step.
  • The precise molecular mechanism of APC-dependent ubiquitination and subunit roles remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of APC-dependent substrate ubiquitination.
  • To investigate the role of the Doc1/Apc10 subunit in APC function.
  • To characterize the impact of Doc1 on APC processivity and substrate affinity.

Main Methods:

  • Utilized a purified Saccharomyces cerevisiae anaphase-promoting complex (APC).
  • Employed a well-defined in vitro system for substrate ubiquitination assays.

Related Experiment Videos

  • Analyzed APC mutants lacking the Doc1/Apc10 subunit (APC(doc1 Delta)).
  • Determined kinetic parameters (apparent K(M)) for substrate binding.

    • Main Results:

    • Highly purified APC demonstrated processive ubiquitination of a model cyclin substrate.
    • APC lacking Doc1 (APC(doc1 Delta)) exhibited reduced processivity.
    • APC(doc1 Delta) showed a significantly increased apparent K(M) for the cyclin substrate.
    • Recombinant Doc1 addition fully restored wild-type APC function.

    Conclusions:

    • Doc1 is essential for APC-mediated ubiquitination processivity.
    • Doc1 enhances processivity by reducing substrate dissociation from the APC.
    • Doc1-related domains may generally promote ubiquitination by increasing substrate-enzyme affinity.