دانلود کتاب The Networking of Chaperones by Co-Chaperones

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Preface Acknowledgements Contents Editors and Contributors Chapter 1: Nucleotide Exchange Factors for Hsp70 Molecular Chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Protei... Introduction Hsp70 Architecture and Functional Cycle DnaK, DnaJ, and GrpE: The Eubacterial Hsp70 System The Evolution of the Eukaryotic Hsp70 Systems Molecular Structure and Function of Eukaryotic NEFs Eukaryotic GrpE Homologs The Hsp110 Family of Nucleotide Exchange Factors Sil1/HspBP1 Homologs BAG Domain-Containing NEFs ADP Dissociation Inhibitors: Antagonists of Hsp70-NEF Function Cellular Functions of NEF Proteins in S. cerevisiae Aspects of NEF Function in Mammalian Protein Folding and Quality Control Conclusions References Chapter 2: Functions of the Hsp90-Binding FKBP Immunophilins Introduction Structure/Function Relationships of Steroid Receptor-Associated FKBPs Cellular and Physiological Functions of Hsp90-Associated FKBPs FKBP52 FKBP51 TPR-Domain Immunophilins Regulate the Subcellular Localization of Soluble Proteins Xap2 FKBP36 FKBP38 FKBPL Plant FKBPs Summary References Chapter 3: Hsp70/Hsp90 Organising Protein (Hop): Coordinating Much More than Chaperones Assisted Protein Folding by the Hsp70/Hsp90 Chaperone Complex Hop (Hsp70-Hsp90 Organising Protein) Structure of Hop Functions of Hop Hop as a Co-chaperone for Hsp70 and Hsp90: A Shift in the Paradigm Extracellular Hop Has Cytokine-Like Activity Hop in Human Cellular Function and Disease Cancer Cell Biology Hop as a Therapeutic Target for Cancer Developmental and Protein Folding Disorders Parasitic Diseases Conclusion References Chapter 4: Specification of Hsp70 Function by Hsp40 Co-chaperones Introduction A. Hsp70 Co-chaperone Activity of Hsp40s B. How Does the J-Domain Regulate Client Binding by Hsp70 C. Do Hsp40s Act as Chaperones? C. Determination of Hsp70 Functional Specificity D. Hsp40 Quaternary Structure E. ER-Transmembrane Hsp40s and Membrane Protein Quality Control F. Hsp40s into the Future References Chapter 5: Cdc37 as a Co-chaperone to Hsp90 Introduction Cdc37 in the Chaperoning of Protein Kinase Structure and Interaction Cdc37 in Cell Proliferation and Cancer Cdc37 and Cancer Treatment Roles for Cdc37 in Autophagy and Protein Aggregation Disorders Conclusions References Chapter 6: p23 and Aha1: Distinct Functions Promote Client Maturation The Conformational Cycle of Hsp90 The Hsp90 Co-chaperone p23 Discovery and Isoforms of p23 The Structure of p23 The Interaction of p23 with Hsp90 p23 and Hsp90 Client Maturation Hsp90-Independent Functions of p23 The Intrinsic Chaperone Function of p23 The Nuclear Function of p23 Concluding Remarks The Hsp90 Co-chaperone Aha1 Discovery and Isoforms of Aha1 The Structure of Aha1 The Interaction of Aha1 with Hsp90 Aha1 and Hsp90 Client Maturation Integration of Aha1 and p23 into the Hsp90 ATPase Cycle Conclusion References Chapter 7: Beyond Chaperoning: UCS Proteins Emerge as Regulators of Myosin-Mediated Cellular Processes Introduction UCS Proteins Are Indispensable for Myosin Folding but not Hsp90 Structural Organization and Versatility of UCS Proteins as Myosin Chaperones UNC-45 Regulates Myosin Expression, Folding, Assembly, Contractile Function, and Degradation UNC-45 Proteins in Invertebrates UNC-45 Proteins in Vertebrates UCS Proteins in Yeasts, Fungi, and Apicomplexans UNC-45 and Cancers Conclusions and Future Work References Chapter 8: Chaperonin: Co-chaperonin Interactions Introduction Activities of the E. coli GroEL/GroES Folding Machine Structure of GroEL and GroES The Role of GroES in the Reaction Cycle Roles of Bacterial Chaperonins Specific Functions of Bacterial Co-chaperonins Roles of Eukaryotic Group I Chaperonins Specific Functions of Eukaryotic Group I Co-chaperonins Conclusion References Chapter 9: Co-chaperones of the Human Endoplasmic Reticulum: An Update Introduction The Chaperone Network of the Mammalian ER The Hsp70/Hsp40 Chaperone Network of the Mammalian ER The Two Hsp70s and NEFs of the Mammalian ER The Functional Cycle of BiP The Co-chaperones of BiP in the Mammalian ER The Dual Role of BiP and Its Co-chaperone Sec63 in Protein Import into the ER as an Example of Chaperone/Co-chaperone Action i... BiP Can Support Opening of the Human Sec61 Channel for ER Protein Import BiP Can Support ER Protein Import by Acting as a Molecular Ratchet on the Incoming Precursor Polypeptide Closing of the Human Sec61 Channel for Preservation of Cellular Calcium Homeostasis Not All Hsp70s Are Created Equal: BiP and Kar2p Cannot Substitute for Each Other in Sec61 Channel Gating Regulatory Mechanisms for the ER-Resident Hsp70/Hsp40 Chaperone Network Nucleotide Transport Into and Out of the ER Human Diseases Related to ER Chaperones or the Sec61 Channel: On Chaperonopathies and Sec61-Channelopathies Conclusions and Open Questions References Chapter 10: J-Domain Proteins Orchestrate the Multifunctionality of Hsp70s in Mitochondria: Insights from Mechanistic and Evol... Introduction The Mitochondrial Hsp70 - Client Polypeptide Binding Cycle Mdj1: Multifunctional JDP that Evolved Mitochondria-Specific Functions Pam18: Specialized JDP that Functions in Protein Import Hsc20: Specialized JDP that Functions in Iron-Sulfur Cluster Biogenesis Evolutionary Dynamics of Mitochondrial JDP/Hsp70 Systems Concluding Remarks References Chapter 11: Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity Introduction The Chaperone Cycle Canonical Co-chaperones Hsp70/Hsp90-Organizing Protein (HOP) Cell Division Cycle 37 (Cdc37) Protein Phosphatase 5 (PP5) Activator of Hsp90 ATPase 1 (Aha1) Prostaglandin E Synthase 3 (p23) Immunophilins SGTA Sgt1 C-Terminus of Hsc70-Interacting Protein (CHIP) New Co-chaperones Folliculin-Interacting Proteins 1 and 2 (FNIP1/2) Tuberous Sclerosis Complex 1 (Tsc1) TIMP-2 Concluding Remarks References Chapter 12: CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome Introduction to Molecular Chaperones and Protein Degradation Protein Degradation via the Proteasome Protein Degradation via Autophagy and the Lysosome The Carboxyl Terminus of Hsp70-Interacting Protein (CHIP) Structure of CHIP Interaction of CHIP with Chaperones and E2 Ligases CHIP Substrates and Human Disease Hsp70 and Hsp90: To Degrade or to Refold? Conclusions References Chapter 13: HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease Introduction The HSP70 Chaperone Machine The HSP90 Chaperone Machine Major Co-chaperones Involved in Both HSP90 and HSP70 Complexes Disruption of Proteostasis and Disease Cooperation of HSP70 and HSP90 Chaperone Machines and Maintenance of Proteostasis in Neurodegenerative Disease Conclusions References Index