Hsp70 chaperones: cellular functions and molecular mechanism.
Matthias P. Mayer,Bernd Bukau +1 more
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TLDR
This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.Abstract:
Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.read more
Citations
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Anaïs Gouin,Anthony Bretaudeau,Anthony Bretaudeau,Kiwoong Nam,Sylvie Gimenez,Jean-Marc Aury,Bernard Duvic,Frédérique Hilliou,Nicolas Durand,Nicolas Montagné,Isabelle Darboux,Suyog S. Kuwar,Thomas Chertemps,David Siaussat,Anne Bretschneider,Yves Moné,Seung-Joon Ahn,Sabine Hänniger,Anne Sophie Gosselin Grenet,David Neunemann,Florian Maumus,Isabelle Luyten,Karine Labadie,Wei Xu,Fotini Koutroumpa,Jean Michel Escoubas,Angel Llopis,Martine Maïbèche-Coisne,Fanny Salasc,Fanny Salasc,Archana Tomar,Alisha Anderson,Sher Afzal Khan,Pascaline Dumas,Marion Orsucci,Julie Guy,Caroline Belser,Adriana Alberti,Benjamin Noel,Arnaud Couloux,Jonathan Mercier,Sabine Nidelet,Emeric Dubois,Nai-Yong Liu,Isabelle Boulogne,Olivier Mirabeau,Gaëlle Le Goff,Karl H.J. Gordon,John G. Oakeshott,Fernando Luis Cônsoli,Anne-Nathalie Volkoff,Howard W. Fescemyer,James H. Marden,Dawn S. Luthe,Salvador Herrero,David G. Heckel,Patrick Wincker,Patrick Wincker,Gael J. Kergoat,Joelle Amselem,Hadi Quesneville,Astrid T. Groot,Astrid T. Groot,Emmanuelle Jacquin-Joly,Nicolas Nègre,Claire Lemaitre,Fabrice Legeai,Emmanuelle d'Alençon,Philippe Fournier +68 more
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Cellular Handling of Protein Aggregates by Disaggregation Machines.
TL;DR: The different chaperone disaggregation machines and their mechanisms of action are reviewed, showing that in all these machines, the coating of protein aggregates by Hsp70 chaperones represents the conserved, initializing step.
References
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TL;DR: Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.
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William B. Pratt,David O. Toft +1 more
TL;DR: This purified system of five purified proteins should facilitate understanding of how eukaryotlc hsp70 and hsp90 work together as essential components of a process that alters the conformations of substrate proteins to states that respond in signal transduction.
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Hsp104, Hsp70, and Hsp40: A Novel Chaperone System that Rescues Previously Aggregated Proteins
John R Glover,Susan Lindquist +1 more
TL;DR: It is concluded that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces.