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- Publisher
- Annual Reviews
- Copyright
- Copyright © 2006 by Annual Reviews. All rights reserved
- ISSN
- 1081-0706
- eISSN
- 1530-8995
- DOI
- 10.1146/annurev.cellbio.22.010605.093503
- pmid
- 16753028
- Publisher site
- See Article on Publisher Site
Abstract
Abstract Following the discovery of protein modification by the small, highly conserved ubiquitin polypeptide, a number of distinct ubiquitin-like proteins (Ubls) have been found to function as protein modifiers as well. These Ubls, which include SUMO, ISG15, Nedd8, and Atg8, function as critical regulators of many cellular processes, including transcription, DNA repair, signal transduction, autophagy, and cell-cycle control. A growing body of data also implicates the dysregulation of Ubl-substrate modification and mutations in the Ubl-conjugation machinery in the etiology and progression of a number of human diseases. The primary aim of this review is to summarize the latest developments in our understanding of the different Ubl-protein modification systems, including the shared and unique features of these related pathways.
Journal
Annual Review of Cell and Developmental Biology – Annual Reviews
Published: Nov 10, 2006