دانلود کتاب Proteostasis and Disease: From Basic Mechanisms to Clinics (Advances in Experimental Medicine and Biology, 1233)

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Preface
Acknowledgments
Contents
Part I: Cancer
Chapter 1: Ubiquitin-Regulated Cell Proliferation and Cancer
1.1 Introduction to Cell Cycle Regulation
1.1.1 Regulation of CDK-Cyclin Activity by the UPS
1.1.2 SCF in Cell Cycle Control
1.1.3 SCF in DNA Damage
1.1.4 APC/C and the Regulation of Mitosis
1.2 Non-proteolytic Protein Ubiquitination in the Control of Cell Cycle Progression
1.2.1 Cell Signaling and Non-proteolytic Protein Ubiquitination in G1
1.2.2 Non-proteolytic Protein Ubiquitination During G1/S to G2 Transition
1.2.3 Non-proteolytic Ubiquitination in Mitosis
1.3 Deregulation of Ubiquitin-Mediated Proteolysis in Cancer
1.3.1 pRb Degradation and Cancer
1.3.2 SCFβ-TrCP, Mdm2, and DNA Damage
1.3.3 SCFβ-TrCP and Colorectal Cancer
1.3.4 SCFSkp2, Cell Cycle Progression, and Cancer
1.3.5 SCFFBXW7 and Cancer
1.3.6 SCFFBXW7, MCL-1, and Apoptosis
1.3.7 APC/C in Cancer
1.4 Targeted Therapy of the Ubiquitin-Proteasome System in Cancer
References
Chapter 2: Ubiquitin, SUMO, and Nedd8 as Therapeutic Targets in Cancer
2.1 Introduction
2.2 Oncogenic and Tumor Suppressor Pathways Are Controlled by UbLs
2.2.1 The p53 Pathway
2.2.2 The NF-κB Pathway
2.2.3 The TGF-β Pathway
2.2.4 PML-RARα in Acute Promyelocytic Leukemias
2.3 Deregulations of UbL Pathways in Cancer
2.3.1 Many UbL Enzymes Are Dysregulated in Cancers
2.3.2 Dysregulation of the Ubiquitin Pathway Enzyme in Cancer
2.3.3 Overactivation of the Nedd8 Pathway in Cancer Is Often Associated with Bad Prognosis
2.3.4 Dysregulations of the SUMO Pathway in Cancer
2.4 Targeting UbLs: New Perspectives in Cancer Treatment
2.4.1 E1 Inhibitors
2.4.1.1 Ubiquitin E1 Inhibitors
2.4.1.2 Nedd8 E1 Inhibitors
2.4.1.3 SUMO E1 Inhibitors
2.4.2 E2 Inhibitors
2.4.3 E3 Inhibitors
2.4.3.1 MDM2 Inhibitors
2.4.3.2 IAP Inhibitors
2.5 Conclusion
References
Chapter 3: The Proteasome System in Health and Disease
3.1 Introduction
3.2 20S Proteasomes: Structure and Regulation
3.2.1 Alternative Composition of the 20S Proteasome
3.2.2 Expression and Assembly of the 20S Proteasome
3.2.3 Activation of the 20S Proteasome
3.2.4 Posttranslational Modifications (PTMs)
3.2.5 Localization
3.3 Proteasome Regulators: Structure and Regulation
3.3.1 19S Regulator and Controlled Assembly of 26S Proteasomes
3.3.1.1 Subcellular Localization of 26S Proteasomes
3.3.1.2 Regulating Abundance of 26S Proteasomes
3.3.1.3 Assembly and Disassembly of 26S Proteasomes
3.3.1.4 Fine-Tuning Activity of 26S Proteasomes by Posttranslational Modifications
3.3.1.5 Regulation of 26S Proteasome by (Transiently) Associated Proteins
ECM29
Ub-Ligases, DUBs Associated to the 26S Proteasome
3.3.2 PA28/REG
3.3.2.1 PA28αβ
3.3.2.2 PA28γ
3.3.3 PA200
3.3.4 PI31
3.4 Proteasomes in Diseased States
3.4.1 Mutations Affecting 20S Proteasome Function
3.4.2 Proteasomes and Oxidative Stress
3.4.3 Cancer
3.4.4 Muscle Atrophy and Hypertrophy
3.4.5 Neurodegenerative Disorders
3.4.6 Cardiovascular Disorders
3.4.7 Respiratory Diseases
3.4.8 Involvement of Individual Proteasome Subunits in Disease
3.5 Modulation of Proteasome Activity in Human Therapy
3.5.1 Proteasome Inhibition
3.5.1.1 Development of Proteasome Inhibitors
3.5.1.2 Proteasome Inhibitors in the Clinic
3.5.2 Activation of the Proteasome in Human Therapy
3.6 Conclusion
References
Chapter 4: Proteostasis Dysregulation in Pancreatic Cancer
4.1 Introduction
4.1.1 High Genetic Variability in PDAC
4.1.2 PDAC Tumor Microenvironment
4.1.3 PDAC Biomarkers
4.2 Intracellular Protein Degradation Systems
4.3 UPS Dysregulation in PDAC
4.3.1 E2 Ubiquitin-Conjugating and E3 Ubiquitin-Ligase Enzymes in PDAC
4.3.2 Deubiquitinating Enzymes in PDAC
4.4 Autophagy Dysregulation in PDAC
4.5 Developing New Therapies Related to Proteostasis
References
Chapter 5: Divergent Modulation of Proteostasis in Prostate Cancer
5.1 Introduction
5.2 Prostate Cancer
5.3 Key Proteins Involved in Prostate Tumorigenesis
5.3.1 Androgen Receptor
5.3.2 Tumor Suppressors
5.3.3 Other Proteins Involved in Prostate Cancer
5.4 Ubiquitin-Related Processes in Prostate Cancer
5.4.1 The Ubiquitin-Mediated Regulation of Androgen Receptor
5.4.2 Regulation of p27, p21, PTEN, and NKX3.1 Tumor Suppressors via E3 Ubiquitin Ligase Enzymes
5.4.3 Other Players of Prostate Cancer and Their Ubiquitin-Mediated Regulations
5.5 The Role of Deubiquitinating Enzymes in Prostate Cancer
5.6 Ubiquitin-Like Modifiers Involved in Prostate Tumorigenesis
5.7 Autophagy and Prostate Cancer
5.8 The Role of Unfolded Protein Response and ERAD in Prostate Cancer
5.9 Conclusion Remarks
References
Chapter 6: Resistance to the Proteasome Inhibitors: Lessons from Multiple Myeloma and Mantle Cell Lymphoma
6.1 Introduction
6.2 Cancers Treated with Proteasome Inhibitors
6.2.1 Multiple Myeloma
6.2.2 Mantle Cell Lymphoma
6.2.3 Proteasomes and Chemical Inhibitors
6.3 Molecular Origin of the Resistance to Bortezomib
6.3.1 Inherent Resistance
6.3.1.1 Mutations in PSMB5 Proteasome Subunit
6.3.1.2 Apoptosis Failure
6.3.1.3 Signalling Cascades
6.3.2 Acquired Resistance
6.3.2.1 Overexpression of Proteasome Subunits
6.3.2.2 Metabolic Adaptation
6.3.2.3 Protein Homeostasis
6.3.2.4 UPS-ALS Crosstalk
6.3.2.5 Stress Signals
6.3.2.6 B Cell Differentiation Programme
6.4 Potential Targets to Recover Proteasome Inhibitors Sensitivity
6.4.1 Deubiquitinases
6.4.2 Transport Modulators
6.4.3 Autophagy Signalling
6.4.4 Oncogenes and Signalling Pathways
6.4.4.1 mTOR/AKT Pathway
6.4.4.2 NF-κB Pathway
6.4.4.3 NOXA/BCL-2 Proteins
6.4.4.4 IRF4/MYC Signalling
6.4.5 Epigenetic Modulators
6.5 Concluding Remarks
References
Part II: Neurodegeneration
Chapter 7: Altered Proteostasis in Neurodegenerative Tauopathies
7.1 Introduction
7.1.1 The Microtubule-Associated Protein Tau
7.1.2 Tauopathies and Tau Toxicity
7.1.3 Proteostatic Failure or Inhibited Proteostasis?
7.2 Proteostatic Mechanisms in Tauopathies
7.2.1 Ubiquitin-Proteasome System and Tau Degradation
7.2.2 Autophagy-Dependent Tau Degradation
7.2.3 Endoplasmic Reticulum-Unfolded Protein Response in Tauopathies
7.3 Synthesis and Perspectives
7.3.1 Failure to Clear Pathogenic Tau or Inhibition of Proteostasis?
7.3.2 Multiplicity of Potential Tau Clearance Mechanisms
7.3.3 Potentially Therapeutic Proteostatic Interventions
References
Chapter 8: The Ubiquitin System in Alzheimer´s Disease
8.1 Alzheimer´s Disease
8.1.1 Dementia
8.1.2 Genome-Wide Association Studies (GWAS)
8.1.3 Molecular Mechanisms in Alzheimer´s Disease
8.1.3.1 Amyloid-Beta (Aβ)
8.1.3.2 Tau
8.1.3.3 Loss of Proteostasis in Alzheimer´s Disease
8.2 The Ubiquitin-Proteasome System
8.2.1 Ubiquitin
8.2.2 Components of the Ubiquitin System
8.2.3 Ubiquitin Signalling and Neuronal Homeostasis
8.3 Ubiquitin Signalling in Alzheimer´s Disease
8.3.1 Ubiquitin and Protein Aggregation
8.3.2 Crosstalk Between Tau, Aβ and Ubiquitin Signalling
8.3.3 Mutant Ubiquitin UBB+1
8.4 Emerging Topics in Proteostasis and Alzheimer´s Disease
8.4.1 Mitochondrial Dysfunction
8.4.2 ER-Mitochondria-Associated Membranes
8.4.3 Necroptosis and Alzheimer´s Disease
8.4.4 Targeting the Ubiquitin System in Alzheimer´s Disease
8.5 Concluding Remarks
References
Chapter 9: The Interplay Between Proteostasis Systems and Parkinson´s Disease
9.1 Introduction
9.2 Parkinson´s Disease
9.3 Regulation of Protein Folding and Aggregation in Mammalian Cells
9.3.1 The Hsp70/Hsp40 System
9.3.2 Hsp90 Chaperone
9.3.3 Small Heat Shock Proteins
9.3.3.1 αB-Crystallin
9.3.3.2 Hsp27
9.4 Proteolytic Recycling of Proteins
9.4.1 The Ubiquitin Proteasome System (UPS)
9.4.2 The Autophagy-Lysosome Pathway (ALP)
9.5 Conclusions and Final Remarks
References
Chapter 10: Machado-Joseph Disease: A Stress Combating Deubiquitylating Enzyme Changing Sides
10.1 Machado-Joseph Disease
10.2 Ataxin-3
10.3 Combating Proteotoxic Stress
10.4 Combating Genotoxic Stress
10.5 Targeting Mutant Ataxin-3 in MJD
10.6 Concluding Remarks
References
Part III: Infection, Inflammation and Developmental Disorders
Chapter 11: SUMO and Cytoplasmic RNA Viruses: From Enemies to Best Friends
11.1 SUMO Conjugation
11.2 Regulation of the Type I Interferon (IFN) Production by SUMO
11.3 SUMO and Type I IFN Responses
11.4 SUMO and RNA viruses
11.4.1 Reoviridae
11.4.2 Paramyxoviridae
11.4.3 Pneumoviridae
11.4.4 Nodaviridae
11.4.5 Picornaviridae
11.4.6 Bunyaviridae
11.4.7 Coronaviridae
11.4.8 Arteriviridae
11.4.9 Filoviridae
11.4.10 Flaviviridae
11.4.11 Rhabdoviridae
11.5 Conclusions
References
Chapter 12: The Role of Proteostasis in the Regulation of Cardiac Intercellular Communication
12.1 The Cardiac Proteostasis Network
12.1.1 Ubiquitin-Proteasome System (UPS)
12.1.2 Autophagy
12.1.2.1 Macroautophagy
12.1.2.2 Autophagy Mediated by Chaperones
12.1.3 Calpain Proteases
12.1.4 Proteolysis Targets in Cardiovascular Diseases
12.2 Intercellular Communication in the Heart
12.2.1 Gap Junctions
12.2.2 Extracellular Vesicles
12.2.3 Tunneling Nanotubes
12.2.4 Intercellular Communication Targets in Cardiovascular Diseases
12.3 Concluding Remarks and Future Perspectives
References
Chapter 13: By the Tips of Your Cilia: Ciliogenesis in the Retina and the Ubiquitin-Proteasome System
13.1 The Retina and Photoreceptors
13.2 Photoreceptor Cilia
13.3 DUBs and the Ubiquitin-Proteasome System (UPS)
13.4 UPS and Ciliogenesis in Replicative Cells
13.5 UPS and Retinal Dystrophies
13.6 Concluding Remarks
References
Chapter 14: TRIM E3 Ubiquitin Ligases in Rare Genetic Disorders
14.1 Introduction
14.2 Genetic Diseases Caused by Mutations in Class I TRIM Genes
14.2.1 TRIM18/MID1 and Opitz G/BBB Syndrome
14.2.2 TRIM1/MID2 and X-Linked Intellectual Disability
14.2.3 TRIM36 and Anencephaly
14.3 Genetic Diseases Caused by Mutations in Class VII TRIM Genes
14.3.1 TRIM2 and Charcot-Marie-Tooth
14.3.2 TRIM32 and Limb Girdle Muscular Dystrophy
14.3.3 TRIM71 and Congenital Hydrocephalus
14.4 Genetic Diseases Caused by Mutations in Other Classes of TRIM Genes
14.4.1 TRIM8 and Epileptic Encephalopathy
14.4.2 TRIM37 and MULIBREY Nanism
14.4.3 RING-less TRIM Family Members and Genetic Diseases
14.4.3.1 TRIM20 and Familial Mediterranean Fever
14.4.3.2 TRIM44 and Aniridia
14.5 Conclusions and Future Perspectives
References
Part IV: Diet
15: We Are What We Eat: Ubiquitin-Proteasome System (UPS) Modulation Through Dietary Products
15.1 Introduction
15.2 The UPS System
15.3 Proteasome Activation
15.4 UPS Modulation in Aging and Neurodegenerative Diseases
15.5 UPS and Diet
15.5.1 Aggregation-Related Disorders
15.5.2 Aging
15.6 Conclusions
References