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- W1570595295 endingPage "441" @default.
- W1570595295 startingPage "429" @default.
- W1570595295 abstract "Ubiquitination is a regulated post-translational modification that conjugates ubiquitin (Ub) to lysine residues of target proteins and determines their intracellular fate. The canonical role of ubiquitination is to mediate degradation by the proteasome of short-lived cytoplasmic proteins that carry a single, polymeric chain of Ub on a specific lysine residue. However, protein modification by Ub has much broader and diverse functions involved in a myriad of cellular processes. Monoubiquitination, at one or multiple lysine residues of transmembrane proteins, influences their stability, protein-protein recognition, activity and intracellular localization. In these processes, Ub functions as an internalization signal that sends the modified substrate to the endocytic/sorting compartments, followed by recycling to the plasma membrane or degradation in the lysosome. E3 ligases play a pivotal role in ubiquitination, because they recognize the acceptor protein and hence dictate the high specificity of the reaction. The multitude of E3s present in nature suggests their nonredundant mode of action and the need for their controlled regulation. Here we give a short account of E3 ligases that specifically modify and regulate membrane proteins. We emphasize the intricate network of interacting proteins that contribute to the substrate-E3 recognition and determine the substrate's cellular fate." @default.
- W1570595295 created "2016-06-24" @default.
- W1570595295 creator A5034849411 @default.
- W1570595295 creator A5037780803 @default.
- W1570595295 creator A5074222588 @default.
- W1570595295 date "2005-04-22" @default.
- W1570595295 modified "2023-10-17" @default.
- W1570595295 title "E3 Ubiquitin Ligases as Regulators of Membrane Protein Trafficking and Degradation" @default.
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