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- Avram Hershko
- Unit of Biochemistry, Faculty of Medicine and the Rappaport Institute for Research in the Medical Sciences, Technion-Israel Institute of Technology, Haifa 31096, Israel
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- Aaron Ciechanover
- Unit of Biochemistry, Faculty of Medicine and the Rappaport Institute for Research in the Medical Sciences, Technion-Israel Institute of Technology, Haifa 31096, Israel
抄録
<jats:p>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.</jats:p>
収録刊行物
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- Annual Review of Biochemistry
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Annual Review of Biochemistry 67 (1), 425-479, 1998-06
Annual Reviews
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キーワード
詳細情報 詳細情報について
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- CRID
- 1363951796177540864
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- NII論文ID
- 80010498322
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- ISSN
- 15454509
- 00664154
- http://id.crossref.org/issn/00664154
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- データソース種別
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