DUBs at a glance.

نویسنده

  • Keith D Wilkinson
چکیده

Introduction The discovery of protein ubiquitylation three decades ago was the beginning of our understanding of a new mechanism by which proteins are marked for assembly into macromolecular complexes or movement between cellular compartments. The finding that ubiquitylation (the covalent attachment of the small protein ubiquitin to other proteins) targeted proteins for degradation earned Avram Hershko, Aaron Ciechanover and Irwin Rose the Nobel Prize in Chemistry in 2004 (Wilkinson, 2004). This early work spawned a large number of studies that investigated the role of ubiquitin and several other ubiquitin-like proteins (UBLs) as targeting signals in virtually all aspects of cellular protein metabolism (Chen, 2005; Cohn and D’Andrea, 2008; Saksena et al., 2007; Weake and Workman, 2008). The best understood example of ubiquitylation is the marking of proteins for delivery to the 26S proteasome, resulting in their degradation (Chiba and Tanaka, 2004; Guo et al., 2007; Hershko and Ciechanover, 1998; Schwartz and Hochstrasser, 2003; Varshavsky et al., 1989).

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عنوان ژورنال:
  • Journal of cell science

دوره 122 Pt 14  شماره 

صفحات  -

تاریخ انتشار 2009