Ubiquitination: RING for destruction?

Ubiquitination: RING for destruction? Ubiquitination targets proteins for degradation and is a potent regulator of cellular protein function. Recent results implicate the RING finger domain in specific ubiquitination events; it is possible that all RING proteins act as E3 ubiquitin protein ligases, with implications for a variety of biological areas. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Biology Elsevier

Ubiquitination: RING for destruction?

Current Biology, Volume 10 (2) – Jan 15, 2000

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Publisher
Elsevier
Copyright
Copyright © 2000 Elsevier Science Ltd
ISSN
0960-9822
D.O.I.
10.1016/S0960-9822(00)00287-6
Publisher site
See Article on Publisher Site

Abstract

Ubiquitination targets proteins for degradation and is a potent regulator of cellular protein function. Recent results implicate the RING finger domain in specific ubiquitination events; it is possible that all RING proteins act as E3 ubiquitin protein ligases, with implications for a variety of biological areas.

Journal

Current BiologyElsevier

Published: Jan 15, 2000

References

  • The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    Xie, Y.; Varshavsky, A.
  • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    Honda, R.; Yasuda, H.

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