Ubiquitylation and Isgylation: Overlapping Enzymatic Cascades Do the Job

Sci. STKE, 10 August 2004
Vol. 2004, Issue 245, p. pe43
DOI: 10.1126/stke.2452004pe43

Ubiquitylation and Isgylation: Overlapping Enzymatic Cascades Do the Job

  1. Olivier Staub*
  1. Department of Pharmacology and Toxicology, University of Lausanne, CH-1005 Lausanne, Switzerland.
  1. *Contact information. Telephone, +41-21-692-5407; fax, +41-21-692-5355; e-mail, olivier.staub{at}ipharm.unil.ch

Abstract

Ubiquitylation—that is, the covalent attachment of ubiquitin polypeptides to target proteins—involves the sequential action of the E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin-protein ligases. Similarly, the conjugation of ubiquitin-like proteins is thought to occur through parallel, but nonidentical, cascades. This concept of strict separation of these modification pathways is now being challenged by the evidence, showing that there are enzymes that play a role both in ubiquitylation and isgylation.

Citation:

O. Staub, Ubiquitylation and Isgylation: Overlapping Enzymatic Cascades Do the Job. Sci. STKE 2004, pe43 (2004).

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