Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
An astounding number of important regulatory and structural proteins are subject to modification by the attachment of ubiquitin or ubiquitin-like proteins. This modification acts as a targeting signal, delivering the modified protein to different locations in the cell and modifying its activity, mac...
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| Published in | The FASEB journal Vol. 11; no. 14; p. 1245 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
United States
01.12.1997
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| Subjects | |
| Online Access | Get more information |
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| Abstract | An astounding number of important regulatory and structural proteins are subject to modification by the attachment of ubiquitin or ubiquitin-like proteins. This modification acts as a targeting signal, delivering the modified protein to different locations in the cell and modifying its activity, macromolecular interactions, or half-life. Deubiquitination, or the removal of this modification, is being recognized as an important regulatory strategy. This reaction is catalyzed by processing proteases known as deubiquitinating enzymes (DUBs). More than 60 DUBs are already known, although little is known about their biological roles. This review concentrates on recent findings and new insights into this fascinating class of enzymes. |
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| AbstractList | An astounding number of important regulatory and structural proteins are subject to modification by the attachment of ubiquitin or ubiquitin-like proteins. This modification acts as a targeting signal, delivering the modified protein to different locations in the cell and modifying its activity, macromolecular interactions, or half-life. Deubiquitination, or the removal of this modification, is being recognized as an important regulatory strategy. This reaction is catalyzed by processing proteases known as deubiquitinating enzymes (DUBs). More than 60 DUBs are already known, although little is known about their biological roles. This review concentrates on recent findings and new insights into this fascinating class of enzymes. |
| Author | Wilkinson, K D |
| Author_xml | – sequence: 1 givenname: K D surname: Wilkinson fullname: Wilkinson, K D organization: Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9409543$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Amino Acid Sequence Animals Biopolymers - chemistry Biopolymers - metabolism Cell Transformation, Neoplastic Endopeptidases - chemistry Endopeptidases - genetics Endopeptidases - metabolism Growth Humans Molecular Sequence Data Morphogenesis Polyubiquitin Protein Processing, Post-Translational Protein Sorting Signals - chemistry Protein Sorting Signals - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Substrate Specificity Thiolester Hydrolases - chemistry Thiolester Hydrolases - genetics Thiolester Hydrolases - metabolism Ubiquitin Thiolesterase Ubiquitins - chemistry Ubiquitins - metabolism |
| Title | Regulation of ubiquitin-dependent processes by deubiquitinating enzymes |
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