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Related Experiment Videos

The APC11 RING-H2 finger mediates E2-dependent ubiquitination.

J D Leverson1, C A Joazeiro, A M Page

  • 1Molecular Biology and Virology Laboratory, The Salk Institute, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.

Molecular Biology of the Cell
|July 11, 2000
PubMed
Summary

The RING-H2 finger protein Apc11 is the minimal ubiquitin ligase for the anaphase-promoting complex (APC), essential for cell viability. Apc11 recruits E2 enzymes and mediates ubiquitination of APC substrates.

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Area of Science:

  • Cellular biology
  • Molecular mechanisms of protein degradation
  • Ubiquitin-proteasome system

Background:

  • Polyubiquitination targets proteins for 26S proteasome degradation via E1, E2, and E3 enzymes.
  • The anaphase-promoting complex/cyclosome (APC/C) is a ubiquitin ligase crucial for cell cycle progression.

Purpose of the Study:

  • To identify the minimal ubiquitin ligase component of the APC.
  • To elucidate the role of Apc11 in APC/C ubiquitin ligase activity.

Main Methods:

  • Investigated the essentiality of the Apc11p RING-H2 finger for yeast cell viability.
  • Used purified recombinant proteins to demonstrate Apc11p interaction with Ubc4 (E2).
  • Assessed Apc11p's ability to mediate ubiquitination of substrates like Clb2p in vitro.

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Main Results:

  • Apc11p's RING-H2 finger integrity is vital for budding yeast cell viability.
  • Apc11p directly interacts with the Ubc4 E2 enzyme.
  • Apc11p catalyzes E1- and E2-dependent ubiquitination of substrates in vitro, independent of Apc2p.

Conclusions:

  • Apc11 defines the minimal ubiquitin ligase activity of the APC.
  • Apc11p likely recruits E2 enzymes and facilitates ubiquitin transfer to APC substrates in vivo.