The ubiquitin system and the N-end rule pathway

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)

URL: http://www.ncbi.nlm.nih.gov/pubmed/11076011
DOI: 10.1515/BC.2000.101

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: http://repository.cshl.edu/id/eprint/27802

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