The Networking of Chaperones by Co-Chaperones
Samenvatting
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is the dynamic integration of the processes of protein folding, degradation and translocation to ensure that cellular function is finely tuned in space and time.
This third edition of the book The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by co-chaperones, a diverse cohort of non-client proteins. Since the second edition was released, not only has knowledge deepened on how co-chaperones act as nodes to network and functionalise chaperones, but an understanding of their broader biological function has started to emerge. The third edition provides new and updated chapters highlighting recent developments and emerging themes on co-chaperones, such as their extracellular functions, their role in human disease and their status as putative drug targets.
The book is a useful resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
Specificaties
Inhoudsopgave
<p> </p>
<p>1. GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones</p>
<p>Andreas Bracher (bracher@biochem.mpg.de) and Jacob Verghese</p>
<p> </p>
<p>2. Functions of the Hsp90-Binding FKBP Immunophilins</p>
<p>Nina R. Ortiz, Naihsuan Guy, Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, and Marc B. Cox (mbcox@utep.edu)</p>
<p> </p>
<p>3. Hsp70/Hsp90 organising protein (Hop): coordinating much more than chaperones</p>
<p>Kelly Schwarz, Swati Baindur-Hudson, Gregory Lloyd Blatch, Adrienne Lesley Edkins (a.edkins@ru.ac.za)</p>
<p> </p>
<p>4. Specification of Hsp70 function by Hsp40 Co-Chaperones</p>
<p>Douglas M. Cyr (dmcyr@med.unc.edu) and Carlos H. Ramos (cramos@iqm.unicamp.br)</p>
<p> </p>
<p>5. Cdc37 as a Co-chaperone to Hsp90</p>
<p>Thomas L Prince, Benjamin J Lang, Yuka Okusha, Takanori Eguchi, Stuart K. Calderwood (scalderw@bidmc.harvard.edu)</p>
<p> </p>
<p>6. p23 and Aha1 – Distinct functions promote client maturation</p>
<p>Maximilian M. Biebl and Johannes Buchner (johannes.buchner@tum.de)</p>
<p> </p>
<p>7. Beyond chaperoning: UCS proteins emerge as regulators of myosin-mediated cellular processes</p>
<p>Odutayo O. Odunuga (odunugaoo@sfasu.edu) and Andres F. Oberhauser (afoberha@utmb.edu)</p>
<p> </p>
<p>8. Chaperonin - Co-Chaperonin Interactions</p>
Aileen Boshoff (a.boshoff@ru.ac.za)<p></p>
<p> </p>
<p>9. Co-chaperones of the human endoplasmic reticulum: an update</p>
Armin Melnyk, Sven Lang, Mark Sicking, Richard Zimmermann (richard.zimmermann@uks.eu) and Martin Jung <p></p>
<p> </p>
<p>10. J Domain Proteins Orchestrate the Multifunctionality of Hsp70s in Mitochondria: Insights from Mechanistic and Evolutionary Analyses</p>
<p>Jaroslaw Marszalek (jmarszalek@wisc.edu), Elizabeth A. Craig (ecraig@wisc.edu) and Bartlomiej Tomiczek</p>
<p> </p>
<p>11. Impact of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity</p>
<p>Sarah J. Backe, Mark R. Woodford, Elham Ahanin, Rebecca A. Sager, Dimitra Bourboulia, Mehdi Mollapour (mollapom@upstate.edu)</p>
<p> </p>
<p>12. CHIP: a co-chaperone for degradation by the proteasome and lysosome.</p>
Abantika Chakraborty and Adrienne L. Edkins (a.edkins@ru.ac.za)<p></p>
<p> </p>
<p>13. HSP70-HSP90 chaperone networking in protein misfolding disease</p>
<p>Chrisostomos Prodromou, Xavi Aran-Guiu, Jasmeen Oberoi, Laura Perna, J. Paul Chapple (j.p.chapple@qmul.ac.uk), and Jacqueline van der Spuy</p>
<p> </p></div><div>Index </div><div><br></div>