Authors: | Streich, F. C.; Lima, C. D. |
Article Title: | Structural and functional insights to ubiquitin-like protein conjugation |
Abstract: | Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regulates numerous cellular processes including transcription, the cell cycle, stress responses, DNA repair, apoptosis, immune responses, and autophagy, to name a few. The mechanistically parallel but functionally distinct conjugation pathways typically require the concerted activities of three types of protein: E1 Ubl-activating enzymes, E2 Ubl carrier proteins, and E3 Ubl ligases. E1 enzymes initiate pathway specificity for each cascade by recognizing and activating cognate Ubls, followed by catalyzing Ubl transfer to cognate E2 protein(s). Under certain circumstances, the E2 Ubl complex can direct ligation to the target protein, but most often requires the cooperative activity of E3 ligases. Reviewed here are recent structural and functional studies that improve our mechanistic understanding of E1-, E2-, and E3-mediated Ubl conjugation. Copyright © 2014 by Annual Reviews. All rights reserved. |
Keywords: | unclassified drug; ubiquitin; protein domain; protein function; protein motif; ubiquitin protein ligase; carboxy terminal sequence; protein protein interaction; enzyme phosphorylation; enzyme regulation; binding site; crystal structure; oxidative stress; conformational transition; autophagy; enzyme specificity; sumo protein; enzyme binding; enzyme structure; ring finger motif; protein cross linking; lysine; disulfide; cysteine; thioester; cullin; protein modification; cyclin dependent kinase 1; enzyme active site; ligase; enzyme conformation; adenylation; conjugation; cyclin dependent kinase 2; anaphase promoting complex; covalent bond; nucleoporin; e3; disulfide bond; e2; ranbp2 protein; nedd8 protein; priority journal; article; e1; ubiquitin-like protein; e1 ubiquitin like protein activating enzyme; e2 ubiquitin like protein conjugating enzyme; e3 ubiquitin like protein ligase |
Journal Title: | Annual Review of Biophysics |
Volume: | 43 |
Issue: | 1 |
ISSN: | 1936-122X |
Publisher: | Annual Reviews |
Date Published: | 2014-05-06 |
Start Page: | 357 |
End Page: | 379 |
Language: | English |
DOI: | 10.1146/annurev-biophys-051013-022958 |
PROVIDER: | scopus |
PUBMED: | 24773014 |
PMCID: | PMC4118471 |
DOI/URL: | |
Notes: | Annu. Rev. Biophys. -- Export Date: 8 July 2014 -- Source: Scopus |