Kerscher_2006 - Modification of Proteins by Ubiquitin and...

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Unformatted text preview: Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins Oliver Kerscher, 1 Rachael Felberbaum, 2 and Mark Hochstrasser 1 , ∗ 1 Molecular Biophysics and Biochemistry, 2 Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06520; email: mark.hochstrasser@yale.edu Annu. Rev. Cell Dev. Biol. 2006. 22:159–80 First published online as a Review in Advance on June 5, 2006 The Annual Review of Cell and Developmental Biology is online at http://cellbio.annualreviews.org This article’s doi: 10.1146/annurev.cellbio.22.010605.093503 Copyright c ° 2006 by Annual Reviews. All rights reserved 1081-0706/06/1110-0159$20.00 ∗ Corresponding author. Key Words sumoylation, neddylation, Ubl conjugation, proteasome, protein degradation 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, includ- ing transcription, DNA repair, signal transduction, autophagy, and cell-cycle control. A growing body of data also implicates the dys- regulation 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 summa- rize the latest developments in our understanding of the different Ubl-protein modification systems, including the shared and unique features of these related pathways. 159 A n n u . R e v . C e l l D e v . B i o l . 2 6 . 2 2 : 1 5 9- 1 8 . D o w n l o a d e d f r o m a r j o u r n a l s . a n n u a l r e v i e w s . o r g b y R I J K S U N I V E R S I T E I T G E N T o n 4 / 1 5 / 8 . F o r p e r s o n a l u s e o n l y . Ubiquitin: a 76-residue protein that is covalently attached to other proteins; it is the founding member of the Ubl protein family Contents INTRODUCTION. . . . . . . . . . . . . . . . . 160 UBL ACTIVATION AND CONJUGATION TO SUBSTRATES . . . . . . . . . . . . . . . . . . 160 UBIQUITIN AND UBL POLYMERS . . . . . . . . . . . . . . . . . . . . . 164 VARIATIONS ON UBL MODIFICATION: EASY AS E1, E2, E3? . . . . . . . . . . . . . . . . . . . . . . 165 Recruiting Substrates . . . . . . . . . . . . . 165 Enzyme Sharing by Ubls. . . . . . . . . . 167 An Exception to the Universal E1-E2 Couple?. . . . . . . . . . . . . . . . 167 TAKING DIRECTIONS FROM UBIQUITIN AND UBLS . . . . . . . 168 Ubiquitin and SUMO-Binding Domains . . . . . . . . . . . . . . . . . . . . . . 168 Ubls and Protein Complex Assembly . . . . . . . . . . . . . . . . . . . . . 170 UBLS AND THEIR CONJUGATION MACHINERY: LOCALIZE TO REGULATE? . . 171 Subcellular Localization of Ubls. . . 171 Localization of the Ubl-Conjugation Machinery . . . 171 NEW FUNCTIONS FOR UBLS . . . 172 SUMO and Ubiquitin in Some Unexpected Places . . . . . . . . . . . . 172 Ubl-Related Pathologies . . . . . . . . . . 173Ubl-Related Pathologies ....
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