| Description |
1 online resource (260 pages) |
| Series |
Protein Degradation Ser |
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Protein Degradation Ser
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| Contents |
Protein Degradation -- Contents -- Preface -- List of Contributors -- 1 Ubiquitin Signaling and Cancer Pathogenesis -- 1.1 Introduction -- 1.1.1 Ubiquitin Signaling Networks -- 1.1.2 Ubiquitin-like Proteins -- 1.2 Ubiquitin in Cancer Pathogenesis -- 1.2.1 Ubiquitin in Cell Cycle Control -- 1.2.2 Ubiquitin in the NF-mB Pathway -- 1.2.3 Ubiquitin as a Signal in DNA Repair -- 1.2.3.1 p53 Pathway -- 1.2.3.2 BRCA1 and FANCD2 -- 1.2.3.3 PCNA and TLS Polymerases -- 1.2.4 Ubiquitin Networks in Angiogenesis -- 1.2.5 Ubiquitin Networks in Receptor Endocytosis -- 1.3 Targeting Ubiquitin Networks in Cancers -- 1.3.1 Targeting Interactions between E3s and their Substrates -- 1.3.2 Targeting the Proteasome -- 1.3.3 Other Approaches -- 1.4 Conclusions and Future Perspectives -- 2 Regulation of the p53 Tumor-suppressor Protein by Ubiquitin and Ubiquitin-like Molecules -- 2.1 Functional Domains of p53 -- 2.2 The Family of Ubiquitin-like Molecules -- 2.3 E3 Ligases for p53 -- 2.4 Modification of p53 with Ubiquitin -- 2.5 Requirements for Mdm2-mediated Ubiquitination of p53 -- 2.6 Regulation of p53 Ubiquitination -- 2.6.1 E2 Conjugating Enzymes -- 2.6.2 Interacting Proteins -- 2.6.3 By Other Post-translational Modifications -- 2.7 De-ubiquitination of p53 -- 2.8 SUMO-1/sentrin/smpt3 -- 2.9 NEDD8/Rub1 -- 2.10 Therapeutic Intervention through the Ubiquitin Pathway -- 3 The Ubiquitin-Proteasome System in Epstein-Barr Virus Infection and Oncogenesis -- 3.1 Introduction -- 3.2 Viral Interference with the Ubiquitin-Proteasome System -- 3.3 The EBV Life Cycle -- 3.4 EBV and the Ubiquitin-Proteasome System -- 3.4.1 EBNA1 -- 3.4.2 EBNA6 (EBNA3C) -- 3.4.3 LMP1 -- 3.4.4 LMP2 -- 3.4.5 BZLF1 (Zta) and BRLF1 (Rta) -- 3.4.6 BPLF1 -- 3.5 EBV-associated Malignancies -- 3.6 Concluding Remarks -- 4 HECT Ubiquitin-protein Ligases in Human Disease -- 4.1 Introduction |
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4.2 Definition of HECT E3s -- 4.3 Human HECT E3s and their Role in Disease -- 4.4 E6-AP -- 4.4.1 E6-AP and Cervical Cancer (Cancer of the Uterine Cervix) -- 4.4.2 E6-AP and Angelman Syndrome -- 4.5 HECTH9 -- 4.6 HECT E3s with WW Domains -- 4.6.1 Nedd4/Nedd4-2 -- 4.6.1.1 Nedd4/Nedd4-2 and Liddle's Syndrome -- 4.6.1.2 Nedd4 and Retrovirus Budding -- 4.6.2 Itch and the Immune Response -- 4.6.3 Smurfs -- 4.6.3.1 Smurfs and Cancer -- 4.6.3.2 Smurfs and Bone Homeostasis -- 4.7 Concluding Remarks -- 5 Ubiquitin-independent Mechanisms of Substrate Recognition and Degradation by the Proteasome -- 5.1 Introduction -- 5.2 Ubiquitin-independent Proteasome Substrates -- 5.2.1 Ornithine Decarboxylase -- 5.2.2 p21(Waf1/Cip1) -- 5.2.3 Retinoblastoma Protein -- 5.2.4 p53 and p73 -- 5.2.5 Human Thymidylate Synthase -- 5.2.6 Rpn4 -- 5.2.7 NF-mB and ImBÜ -- 5.2.8 Steroid Receptor Co-activator-3 -- 5.2.9 c-Jun -- 5.3 Mechanisms of Ubiquitin-independent Degradation -- 5.4 Conclusion -- 6 Endoplasmic Reticulum Protein Quality Control and Degradation -- 6.1 Introduction -- 6.2 ER-import, Folding and the Unfolded Protein Response -- 6.3 General Principles and Components of ERQD (Endoplasmic Reticulum Quality Control and Protein Degradation) -- 6.4 Mechanism of ERQD -- 6.5 "Overflow" Degradation Pathways: ER-to-Golgi Transport and Autophagocytosis -- 6.6 The Retrotranslocation Channel -- 6.7 Metazoan ERQD -- 7 Interactions between Viruses and the Ubiquitin-Proteasome System -- 7.1 Introduction -- 7.2 Overview of Viruses and the Ubiquitin-Proteasome System -- 7.2.1 Proteolysis -- 7.2.2 Viruses and the ERAD Pathway -- 7.2.3 Membrane Protein Trafficking and Endosomal Sorting -- 7.2.4 Viral Entry and Egress -- 7.2.5 Transcriptional Regulation -- 7.2.6 Cell Cycle Control -- 7.2.7 Cell Signaling -- 7.3 Viruses and E3 Ubiquitin-Protein Ligases |
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7.3.1 ICP0 -- A Viral RING E3 Ligase in HSV Activation -- 7.3.2 Preventing the Release of Interferon -- 7.3.3 Viral E3 Ligases Ubiquitinate and Dispose of Critical Immune Receptors -- 7.3.4 Degradation of MHC Class I Molecules by the mK3 Protein of MHV-68 Virus -- 7.3.5 Degradation of Immunoreceptors by Kaposi's Sarcoma-associated Herpesvirus -- 7.3.6 Viral SCF E3 Ligases -- 7.3.7 HIV Vif and APOBEC Function -- 7.3.8 Viral Recruitment of E3 Ligases -- 7.4 Conclusions -- 8 The Ubiquitin-Proteasome System in Parkinson's Disease -- 8.1 Introduction -- 8.2 Protein Handling in the CNS -- 8.3 The UPS and Protein Mishandling in PD -- 8.4 Parkin -- 8.5 UCH-L1 -- 8.6 Ü-Synuclein -- 8.7 Dardarin/LRRK2 -- 8.8 PINK1 -- 8.9 DJ-1 -- 8.10 Proteasomal Dysfunction in Sporadic PD -- 8.10.1 Altered Proteasomal Function -- 8.10.2 Role of Proteasomal Dysfunction in the Neurodegenerative Process -- 8.10.3 The Cause of Proteasomal Dysfunction -- 8.11 Conclusion -- 9 The Molecular Pathway to Neurodegeneration in Parkin-Related Parkinsonism -- 9.1 Introduction -- 9.2 Parkin is an E3 Ubiquitin Ligase -- 9.2.1 Parkin and the Ubiquitin-Proteasome System -- 9.2.2 Proteasome-independent Role of Parkin -- 9.2.3 Multiple Monoubiquitination is Mediated by Parkin -- 9.2.4 Modulators of Parkin E3 Activity -- 9.3 Substrates of Parkin -- 9.3.1 Parkin Substrates and their Recognition Mechanisms -- 9.3.2 The Link between Substrate Accumulation and Cell Death: Pael-R -- 9.3.2.1 Pael-R and Endoplasmic Reticulum Stress -- 9.3.2.2 Pael-R Overexpressing Animals and Dopaminergic Neurodegeneration -- 9.3.3 The Link between Substrate Accumulation and Cell Death: CDC-rel1, Synphilin-1, Cyclin E and p38 -- 9.4 The Animal Models of AR-JP -- 9.4.1 Drosophila Model of AR-JP -- 9.4.2 Parkin-null Drosophila and Drosophila -- 9.4.3 Mouse Model of AR-JP -- 9.4.4 The Problems with Animal Models of AR-JP |
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9.5 Future Directions -- 10 Parkin and Neurodegeneration -- 10.1 Introduction -- 10.2 AR JP and Parkin -- 10.2.1 ARJP: Introduction -- 10.2.2 PARKIN: The Gene -- 10.2.3 PARKIN: Localization and Regulation -- 10.3 Parkin in the Ubiquitin-Proteasome Pathway -- 10.3.1 The Ubiquitin-Proteasome Pathway -- 10.3.2 PARKIN: An E3 Ubiquitin Ligase -- 10.3.3 Parkin and Lewy Bodies -- 10.3.4 Parkin Substrates -- 10.4 Parkin in Neuroprotection -- 10.4.1 Toxic Parkin Substrates -- 10.4.2 Stress-mediated Toxicity -- 10.5 Parkin and Other PD-linked Genes -- 10.5.1 Ü-Synuclein -- 10.5.2 DJ-1 -- 10.5.3 LRRK2 -- 10.6 Mechanisms of Parkin Dysfunction -- 10.6.1 Pathogenic Mutations -- 10.6.2 Cellular Regulators of Parkin -- 10.6.3 Post-translational Regulation of Parkin -- 10.7 Animal Models of Parkin Deficiency -- 10.7.1 Drosophila Models -- 10.7.2 Mouse Models -- 10.8 Concluding Remarks -- Index |
| Summary |
This final volume in the series focuses on malfunctions of the ubiquitin-proteasome system and their role in human disease. The editors and authors represent unmatched expertise, comprising virtually all the top scientists in the field, including the pioneers of protein degradation research. From the contents: * Ubiquitin and cancer * Ubiquitin and liver cancer * Muscle atrophy * Aggresomes and human disease * Parkin and neurodegeneration * Chronic neurodegenerative diseases * Parkinson's disease * Ubiquitin and viruses * Druggability of the ubiquitin-proteasome system Required reading for molecular and cell biologists, as well as physiologists with an interest in the topic |
| Notes |
Publisher supplied metadata and other sources |
| Subject |
Cell physiology.
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Proteins -- Metabolism.
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Ubiquitin -- Physiology.
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Ubiquitin.
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| Form |
Electronic book
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| Author |
Ciechanover, Aaron J.
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Rechsteiner, Martin.
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| ISBN |
3527620303 |
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9783527620302 (electronic bk.) |
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