泛素
生物
泛素结合酶
脱氮酶
计算生物学
蛋白质组
细胞生物学
泛素蛋白连接酶类
泛素连接酶
蛋白质组学
生物信息学
生物化学
基因
作者
Michael J. Clague,Claire Heride,Sylvie Urbé
标识
DOI:10.1016/j.tcb.2015.03.002
摘要
•Global proteome analysis provides an inventory of the ubiquitin system. •DUBs and E2s both outnumber RING E3s. •Key ubiquitin linkage-specific enzymes have been identified. The ubiquitin system is a major coordinator of cellular physiology through regulation of both protein degradation and signalling pathways. A key building block of a systems-level understanding has been generated by global proteomic studies, which provide copy number estimates for each component. The aggregate of ubiquitin, conjugating enzymes (E1, E2, and E3s), and deubiquitylases (DUBs) represents ∼1.3% of total cellular protein. Complementary approaches have generated quantitative measurements of various ubiquitin pools and further subdivision into different ubiquitin chain topologies. Systematic studies aimed at associating specific enzymes (E2s and DUBs) with the dynamics of these different pools have also made significant progress. Here, we delineate the emerging picture of the most significant determinants of the cellular ubiquitin economy. The ubiquitin system is a major coordinator of cellular physiology through regulation of both protein degradation and signalling pathways. A key building block of a systems-level understanding has been generated by global proteomic studies, which provide copy number estimates for each component. The aggregate of ubiquitin, conjugating enzymes (E1, E2, and E3s), and deubiquitylases (DUBs) represents ∼1.3% of total cellular protein. Complementary approaches have generated quantitative measurements of various ubiquitin pools and further subdivision into different ubiquitin chain topologies. Systematic studies aimed at associating specific enzymes (E2s and DUBs) with the dynamics of these different pools have also made significant progress. Here, we delineate the emerging picture of the most significant determinants of the cellular ubiquitin economy. a process in which a portion of cytoplasm is engulfed by a specific membrane and later degraded following fusion with lysosomes. a class of enzymes that cleave ubiquitin from modified substrate proteins. a multisubunit protease involved in the removal of the ubiquitin-like protein NEDD8 from Cullin-RING E3 ligase complexes. a remnant peptide derived from trypsin treatment of ubiquitylated proteins. It is used in proteomics studies as a signature of ubiquitylation. a pathway that allows the delivery of contents from the cell exterior or secretory pathway to the lysosome through intermediate compartments. The lysosome contains more than 50 acid hydrolases, which can digest major macromolecular components of the cell. multicatalytic protein complex involved in the degradation of ubiquitylated cytosolic proteins. covalent link between a sulfur and an acyl group. a 76-amino acid protein that can be post-translationally conjugated to substrate proteins, normally at Lys residues. also known as ubiquitin-activating enzymes. These enzymes use ATP to activate ubiquitin and then transfer it to an E2 enzyme. also known as ubiquitin-conjugating enzymes. These enzymes receive ubiquitin from the ubiquitin E1 and catalyse the transfer to a substrate protein or to a subset of E3s. also known as ubiquitin-ligase enzymes. These proteins select targets for ubiquitylation and stimulate the conjugation reaction.
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