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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity

Vanja Nagy
  • Mediterranean Institute of Life Sciences, Tumor Biology Program, Mestrovicevo setaliste bb, HR-21000 Split, Croatia
  • Department of Biology, Faculty of Science, University of Split, Teslina 12, HR-21000 Split, Croatia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Ivan Dikic
  • Mediterranean Institute of Life Sciences, Tumor Biology Program, Mestrovicevo setaliste bb, HR-21000 Split, Croatia
  • Institute of Biochemistry II, Johann Wolfgang Goethe University School of Medicine, D-60590 Frankfurt/Main, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-12-23 | DOI: https://doi.org/10.1515/bc.2010.021

Abstract

Localization, activity and lifespan of a protein are signaled by a small, 8 kDa protein, ubiquitin (Ub). Ub conjugation is a post-translational modification orchestrated by the sequential action of activating (E1), conjugating (E2), and ligating (E3) enzymes. Although a simple combination of an E2 and an E3 enzyme can be sufficient for an active complex, in other cases ubiquitination can occur in the context of large multimeric complexes with enhanced molecular abilities. Here, we review several Ub ligase complexes to highlight strategies governing conjugational specificity, the gained adaptability in substrate specificity, and modulatory flexibility encoded in regulatory components of these diverse multimers.

Keywords: APC/C; E2 enzyme; E3 enzyme; LUBAC; parkin; SCF; ubiquitination

About the article

Corresponding authors ;


Received: 2009-09-15

Accepted: 2009-12-03

Published Online: 2009-12-23

Published in Print: 2010-01-01


Citation Information: Biological Chemistry, Volume 391, Issue 2/3, Pages 163–169, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.021.

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