Abstract
The post-translational modification of proteins by covalent attachment of ubiquitin targets these proteins for degradation by the proteasome. An astounding number of proteins are involved in ubiquitination and deubiquitination of proteins. The pathways are combinatorial, and selectivity of proteolysis will depend strongly on the exact combination of ubiquitinating and deubiquitinating enzymes present at any time. In addition to temporal control, it is likely that these modifications are also regulated spatially. In this review, we discuss the regulation of ubiquitination by enzymes of this pathway and highlight some of the outstanding problems in understanding this regulation.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Cysteine Endopeptidases / metabolism*
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Enzyme Activation
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Humans
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Hydrolases / metabolism*
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Ligases / metabolism
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Multienzyme Complexes / metabolism*
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Phosphorylation
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Proteasome Endopeptidase Complex
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Protein Precursors / metabolism
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Protein Processing, Post-Translational*
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Protein Sorting Signals
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Proteins / metabolism*
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Thiolester Hydrolases / metabolism
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Ubiquitin Thiolesterase
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Ubiquitins / metabolism*
Substances
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Multienzyme Complexes
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Protein Precursors
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Protein Sorting Signals
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Proteins
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Ubiquitins
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Hydrolases
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Thiolester Hydrolases
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Ubiquitin Thiolesterase
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Ligases