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The ubiquitin system
Author(s): Hershko A, Ciechanover A
Source: ANNUAL REVIEW OF BIOCHEMISTRY    Volume: 67    Pages: 425-479    Published: 1998  
Times Cited: 3,063     References: 302     
Abstract: The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes, including cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, and endocytosis. The ubiquitin system has been implicated in the immune response, development, and programmed cell death. Abnormalities in ubiquitin-mediated processes have been shown to cause pathological conditions, including malignant transformation. In this review we discuss recent information on functions and mechanisms of the ubiquitin system. Since the selectivity of protein degradation is determined mainly at the stage of ligation to ubiquitin, special attention is focused on what we know, and would like to know, about the mode of action of ubiquitin-protein ligation systems and about signals in proteins recognized by these systems.
Document Type: Review
Language: English
Reprint Address: Hershko, A (reprint author), Technion Israel Inst Technol, Fac Med, Biochem Unit, IL-31096 Haifa, Israel
Addresses:
1. Technion Israel Inst Technol, Fac Med, Biochem Unit, IL-31096 Haifa, Israel
2. Technion Israel Inst Technol, Rappaport Inst Res Med Sci, IL-31096 Haifa, Israel
Publisher: ANNUAL REVIEWS INC, 4139 EL CAMINO WAY, PO BOX 10139, PALO ALTO, CA 94303-0139 USA
Subject Category: Biochemistry & Molecular Biology
IDS Number: 116JT
ISSN: 0066-4154
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