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
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Proteotoxicity from aberrant ribosome biogenesis compromises cell fitness
Blake Tye,Nicoletta Commins,Lillia V. Ryazanova,Martin Wühr,Michael Springer,David Pincus,David Pincus,L. Stirling Churchman +7 more
TL;DR: It is proposed that ribosome assembly is a key vulnerability of proteostasis maintenance in proliferating cells that may be compromised by diverse genetic, environmental, and xenobiotic perturbations that generate orphan r-proteins.
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Cysteine Reactivity Distinguishes Redox Sensing by the Heat-Inducible and Constitutive Forms of Heat Shock Protein 70
Yoshinari Miyata,Jennifer N. Rauch,Umesh K. Jinwal,Andrea D. Thompson,Sharan R. Srinivasan,Chad A. Dickey,Jason E. Gestwicki +6 more
TL;DR: It is reported that MB irreversibly inactivates Hsp72 but not the nearly identical, constitutively expressed isoform, heat shock cognate 70 (Hsc70; HSPA8), which suggests that redox sensing by specific cysteine residues in Hsc72, but not Hsc70, may be an important component of the chaperone response to oxidative stress.
Journal ArticleDOI
Enhanced Immunogenicity of Heat Shock Protein 70 Peptide Complexes from Dendritic Cell-Tumor Fusion Cells
Yutaka Enomoto,Ajit Bharti,Ad Abdul Khaleque,Baizheng Song,Chunlei Liu,Vasso Apostolopoulos,Pei-Xiang Xing,Stuart K. Calderwood,Jianlin Gong +8 more
TL;DR: These experiments indicate that HSP70-peptide complexes (PC) derived from DC-tumor fusion cells have increased their immunogenicity and therefore constitute an improved formulation of chaperone protein-based tumor vaccine.
Journal ArticleDOI
A plastid-targeted heat shock cognate 70 kDa protein interacts with the Abutilon mosaic virus movement protein
TL;DR: Although AbMV DNA accumulated within chlorotic spots, a spatial restriction of these occurred, suggesting a functional relevance of the MP-chaperone interaction for viral transport and symptom induction.
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Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication.
TL;DR: The results of this study reconciled structural and functional experiments from a network-centric perspective by showing that global properties of the residue interaction networks and coevolutionary signatures may be linked with specificity and diversity of allosteric regulation mechanisms.
References
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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.