Varshavsky, A., Turner, G., Du, F., Xie, Y. (2000) The ubiquitin system and the N-end rule pathway. Biological Chemistry, 381 (9-10). pp. 779-789. ISSN 14316730 (ISSN)
Abstract
Eukaryotes contain a highly conserved multienzyme system which covalently links a small protein, 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, an ATP-dependent protease. Pathways that involve ubiquitin play major roles in a huge variety of processes, including cell differentiation, cell cycle, and responses to stress. In this article we briefly review the design of the ubiquitin system, and describe two recent advances, the finding that ubiquitin ligases interact with specific components of the 26S proteasome, and the demonstration that peptides accelerate their uptake into cells by activating the N-end rule pathway, one of several proteolytic pathways of the ubiquitin system.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | E3 N-end rule Peptide import Proteasome Proteolysis Ubiquitin adenosine triphosphate cell protein ligase multienzyme complex peptide proteinase amino terminal sequence animal cell article cell activation cell cycle cell differentiation cell function conjugation controlled study covalent bond eukaryote mouse nonhuman priority journal protein analysis protein degradation protein protein interaction protein transport Saccharomyces cerevisiae stress animal awards and prizes biochemistry eukaryotic cell Germany human physiology review signal transduction Animals Cell Physiology Eukaryotic Cells Humans Ubiquitins |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > ubiquitin ligase |
| CSHL Authors: | |
| Communities: | CSHL labs > Turner lab |
| Depositing User: | Matt Covey |
| Date: | 2000 |
| Date Deposited: | 14 Mar 2013 15:40 |
| Last Modified: | 14 Mar 2013 15:40 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/27802 |
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