Ubiquitin-like protein conjugation: Structures, chemistry, and mechanism Journal Article


Authors: Cappadocia, L.; Lima, C. D.
Article Title: Ubiquitin-like protein conjugation: Structures, chemistry, and mechanism
Abstract: Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin, conjugation is achieved through a cascade of activities that are catalyzed by El activating enzymes, E2 conjugating enzymes, and E3 ligases. In this review, we will sumrnarize structural and mechanistic details of enzymes and protein cofactors that participate in Ubl conjugation cascades. Precisely, we will focus on conjugation machinery in the SUMO, NEDD8, ATG8, ATG12, URM1, UFM1, FAT10, and ISG15 pathways while referring to the ubiquitin pathway to highlight common or contrasting themes. We will also review various strategies used to trap intermediates during Ubl activation and conjugation.
Keywords: crystal-structure; e3 ligase activity; in-vitro reconstitution; complex reveals; chain formation; activating enzyme; atg12-atg5 conjugate; e2 enzyme; sumo-binding-motif; modifier 1 sumo1
Journal Title: Chemical Reviews
Volume: 118
Issue: 3
ISSN: 0009-2665
Publisher: American Chemical Society  
Date Published: 2018-02-14
Start Page: 889
End Page: 918
Language: English
ACCESSION: WOS:000425474300002
DOI: 10.1021/acs.chemrev.6b00737
PROVIDER: wos
PMCID: PMC5815371
PUBMED: 28234446
Notes: Review -- SI -- Source: Wos
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  1. Christopher D Lima
    103 Lima