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Ubiquitin enters the new millennium.

Molecular cell·2001
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Distinct functional surface regions on ubiquitin.

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Related Experiment Video

Updated: Feb 6, 2026

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
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Mechanisms underlying ubiquitination.

C M Pickart1

  • 1School of Public Health, Johns Hopkins University, 615 North Wolfe Street, Baltimore, Maryland 21205, USA. cpickart@welchlink.welch.jhu.edu

Annual Review of Biochemistry
|June 8, 2001
PubMed
Summary

Ubiquitin ligases (E3s) control cell functions by attaching ubiquitin to proteins. Recent studies reveal their catalytic domains (HECT, RING) and active sites, advancing understanding of E3 enzyme mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Ubiquitin conjugation regulates diverse eukaryotic cellular functions.
  • Ubiquitin-protein ligases (E3s) mediate ubiquitination with high efficiency and selectivity.
  • E3s recognize substrates via specific signals and catalyze ubiquitin-protein isopeptide bond formation.

Purpose of the Study:

  • To elucidate the molecular mechanisms of catalysis by E3 enzymes.
  • To understand the structure and function of E3 catalytic domains.
  • To provide detailed views of E3 active sites.

Main Methods:

  • Analysis of E3 enzyme specificity.
  • Structural studies, including crystal structures of HECT and RING finger domains.
  • Biochemical characterization of E3 catalytic activity.

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Main Results:

  • All known E3s employ either a HECT or a RING finger catalytic domain.
  • Crystal structures provide detailed insights into the active sites of both HECT and RING finger E3s.
  • New findings illuminate various aspects of E3 structure, function, and mechanism.

Conclusions:

  • E3 enzymes utilize conserved catalytic domains (HECT, RING) for substrate ubiquitination.
  • Structural data offers a mechanistic basis for E3 specificity and catalysis.
  • Despite advances, key features of E3 catalysis require further investigation.