The Networking of Chaperones by Co-chaperones : Control of Cellular Protein Homeostasis
Gregory. Blatch
Bok Engelsk 2015 · Electronic books.
| Annen tittel | |
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| Utgitt | Dordrecht : Springer , cop. 2015
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| Omfang | 1 online resource (286 p.)
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| Opplysninger | Description based upon print version of record.. - Preface ; Acknowledgements; Contents; Contributors; About the Editors; Chapter 1; GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG Domain Proteins: Nucleotide Exchange Factors for Hsp70 Molecular Chaperones; Introduction; Hsp70 Architecture and Functional Cycle; DnaK, DnaJ and GrpE: The Eubacterial Hsp70 System; The Evolution of 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; Antagonism Between Hip and NEFs. - Assisted-Protein Folding by the Hsp70/Hsp90 Chaperone ComplexHop (Hsp70-Hsp90 Organising Protein); Structure of Hop; Functions of Hop; Hop as a Co-chaperone for Hsp70 and Hsp90; Extracellular Hop has Cytokine-like Activity; Hop in Human Cellular Function and Disease; Cancer Cell Biology; Developmental and Protein Folding Disorders; Parasitic Diseases; Conclusion; References; Chapter 4; Specification of Hsp70 Function by Type I and Type II Hsp40; Introduction; Hsp70 Co-Chaperone Activity of Hsp40s; Do Hsp40s Act as Chaperones?; Determination of Functional Specificity; The G/F Region. - Cellular Functions of NEF Proteins in S. cerevisiaeAspects 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; Cytoplasmic Transport; Xap2; FKBP36; FKBP38; FKBPL; Plant FKBPs; Summary; References; Chapter 3; Hsp70/Hsp90 Organising Protein (Hop): Beyond Interactions with Chaperones and Prion Proteins. - Central DomainsSubstrate Binding Domains; Hsp40 Quaternary Structure; References; Chapter 5; Cdc37 as a Co-chaperone to Hsp90; Introduction; Posttranslational Modifications of Cdc37 and Hsp90; 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; The Hsp90 ATPase Cycle; The Cochaperone p23; Discovery and Occurrence; Structure; Functions of p23; Interaction with Hsp90; How p23 Assists Hsp90 in Client Protein Folding; Hsp90 Independent Functions. - The Function of p23 as a ChaperoneNuclear Functions of p23; The Cochaperone Aha1; Discovery and Occurrence; Structure; Functions of Aha1; Interaction with Hsp90; Client Protein Activation; The Interplay Between p23 and Aha1 in the Hsp90 Cycle; Conclusions; References; Chapter 7; UCS Proteins: Chaperones for Myosin and Co-Chaperones for Hsp90; Introduction; Myosin Folding and Assembly are Chaperone-Dependent Processes; UCS Proteins-Hsp90 Interaction in Myosin Folding, Assembly and Function; Structural Organization and Versatility of UCS Proteins as Myosin Chaperones. - UNC-45 Proteins in Invertebrates. - Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-ch
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| Emner | |
| Sjanger | |
| Dewey | |
| ISBN | 9783319117300
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