Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks

• Συγγραφή απο Οργανισμό/Αρχή: SpringerLink (Online service)
• Άλλοι συγγραφείς: Csermely, Peter (Επιμελητής έκδοσης), Vígh, László (Επιμελητής έκδοσης)
• Μορφή: Ηλεκτρονική πηγή Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: New York, NY : Springer New York, 2007.
• Σειρά: Advances in Experimental Medicine and Biology, 594
• Θέματα: Life sciences.; Immunology.; Biochemistry.; Cell biology.; Biophysics.; Biological physics.; Life Sciences.; Biochemistry, general.; Cell Biology.; Biophysics and Biological Physics.

 We are extremely happy to present the reader this book containing a summary of a well-known research field, the phenomenon of cellular stress defense from two new angles: networks and membranes. The volume starts with an introduction to the concept of molecular chaperones in their original sense: R. John Ellis, the founder of the chaperone concept describes chaperones as mediators of correct assembly and/or misassembly of other macromolecular complexes. This sets the tone of the book, where later chapters give detailed examples of the richness of chaperone ac­ tion by hundreds of other proteins and membrane structures. The reader will learn the role of chaperone classes such as Hsp27 or Hsp90, the action of highly organized chaperone networks in various cellular compartments such as the ER or mitochondrial/ER networks as well as the molecular details of the signaling mechanisms leading to chaperone induction during stress. Various special stress defense mechanisms against oxidative stress or dryness will also be covered. Membranes comprise a surprising mixture of stability and dynamics in the cell. Their role in the regulation of the stress response has been accepted only slowly in the field. Two chapters summarize this important aspect of the stress response showing the importance of membrane hyperstructures, lipid species composition, protein/ membrane interactions and cold adaptation. 

 Protein Misassembly -- The Cellular “Networking” of Mammalian Hsp27 and Its Functions in the Control of Protein Folding, Redox State and Apoptosis -- Molecular Interaction Network of the Hsp90 Chaperone System -- Organization of the Functions and Components of the Endoplasmic Reticulum -- Molecular Crime and Cellular Punishment -- Chaperones as Parts of Cellular Networks -- Chaperones as Parts of Organelle Networks -- Heat Shock Factor 1 as a Coordinator of Stress and Developmental Pathways -- Chaperone Regulation of the Heat Shock Protein Response -- Mechanisms of Activation and Regulation of the Heat Shock-Sensitive Signaling Pathways -- Membrane-Regulated Stress Response -- Beyond the Lipid Hypothesis -- Trehalose As a “Chemical Chaperone” -- Chaperones As Part of Immune Networks -- The Stress of Misfolded Proteins -- Hsp90 and Developmental Networks.