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Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins [PDF]
Annual Review of Cell and Developmental Biology, 2006 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, including transcription ...
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Annual Review of Biochemistry, 2012
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David Komander, Michael Rape
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The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David Komander, Michael Rape
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Trends in Biochemical Sciences, 1997
Eukaryotes contain a highly conserved multi-enzyme system that covalently links ubiquitin to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, a large ATP-dependent protease.
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Eukaryotes contain a highly conserved multi-enzyme system that covalently links ubiquitin to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, a large ATP-dependent protease.
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Ubiquitin and Ubiquitin-like Modifiers in Plants
Journal of Plant Biology, 2011Posttranslational modifications of proteins by small polypeptides including ubiquitination, neddylation (related to ubiquitin (RUB) conjugation), and sumoylation are implicated in plant growth and development, and they regulate protein degradation, location, and interaction with other proteins.
Hans J. Bohnert +5 more
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Is This Protein Ubiquitinated?
2005Covalent modification of proteins with ubiquitin plays an important role in a wide array of cellular processes (Hershko and Ciechanover, 1998; Pickart, 2004). For this reason an increasing number of investigators in diverse research fields are confronted with the question whether their favorite proteins are ubiquitinated.
Christian Tagwerker, Peter K. Kaiser
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The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
Trends in Biochemical Sciences, 2017The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate (monoubiquitination), ubiquitin can itself be ubiquitinated on any of its seven lysine (Lys) residues or its N-terminal methionine (Met1).
Aaron Ciechanover +2 more
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Targeting the monocytic ubiquitin system with extracellular ubiquitin
Immunology & Cell Biology, 2006Recent findings suggest that extracellular ubiquitin has pleiotropic effects on host defence mechanisms, but its cellular mechanism of action is not yet understood. Using fluorescence and in vivo confocal microscopy, we observed uptake of Nâterminal fluoresceinâlabelled ubiquitin into human PBMC and MonoMac 6 cells. Immunoblotting experiments indicated
Thomas Hirsch +2 more
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Trends in Biochemical Sciences, 2000
The ubiquitin-proteasome system fulfills an essential function in eukaryotes by controlling the levels of crucial intracellular regulatory proteins. In this system, a specific type of polyubiquitin chain acts as the proximal signal for targeting substrates to 26S proteasomes for degradation.
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The ubiquitin-proteasome system fulfills an essential function in eukaryotes by controlling the levels of crucial intracellular regulatory proteins. In this system, a specific type of polyubiquitin chain acts as the proximal signal for targeting substrates to 26S proteasomes for degradation.
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Ubiquitin and ubiquitin-like proteins as multifunctional signals
Nature Reviews Molecular Cell Biology, 2005Protein ubiquitylation is a recognized signal for protein degradation. However, it is increasingly realized that ubiquitin conjugation to proteins can be used for many other purposes. Furthermore, there are many ubiquitin-like proteins that control the activities of proteins.
Colin Gordon +2 more
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