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Title:
The Hsp70 chaperone network | Nature Reviews Molecular Cell Biology
Description:
The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a large variety of cellular protein folding and remodelling processes. They function virtually at all stages of the life of proteins from synthesis to degradation and are thus crucial for maintaining protein homeostasis, with direct implications for human health. A large set of co-chaperones comprising J-domain proteins and nucleotide exchange factors regulate the ATPase cycle of Hsp70s, which is allosterically coupled to substrate binding and release. Moreover, Hsp70s cooperate with other cellular chaperone systems including Hsp90, Hsp60 chaperonins, small heat shock proteins and Hsp100 AAA+ disaggregases, together constituting a dynamic and functionally versatile network for protein folding, unfolding, regulation, targeting, aggregation and disaggregation, as well as degradation. In this Review we describe recent advances that have increased our understanding of the molecular mechanisms and working principles of the Hsp70 network. This knowledge showcases how the Hsp70 chaperone system controls diverse cellular functions, and offers new opportunities for the development of chemical compounds that modulate disease-related Hsp70 activities. The Hsp70 chaperones regulate protein metabolism, including folding, unfolding, subcellular localization, aggregation/disaggregation and incorporation into protein complexes. Recent studies have revealed the mechanisms of functions of Hsp70s and their co-chaperones, highlighting new opportunities for modulating disease-related Hsp70 roles.
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pubmed, article, google, scholar, cas, hsp, central, biol, protein, chaperone, mol, cell, molecular, chaperones, proteins, chem, nature, dnak, nat, binding, substrate, bukau, mayer, domain, function, folding, sci, structure, struct, heat, shock, mechanism, dnaj, disaggregation, nucleotide, hsc, peptide, cellular, structural, aggregates, role, stress, acad, cochaperone, nillegoda, degradation, exchange, regulation, aggregation, access,
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atp-bound open conformation nature portfolio journals permissions reprints hsp70-regulated mild-photothermal therapy nature portfolio privacy policy author information authors characteristic cross-β-sheet motifs advertising research grant glycine-phenylalanine-rich region determines j-domain-triggered atp hydrolysis social media research age-related muscle decline small heat shock proteins atp hydrolysis-dependent manner distance-dependent energy transfer nature+ nature 346 nature 539 nature 524 nature 561 nature 378 nature 432 nature uncoating clathrin-coated vesicles sil1-bip complex reveals atp-dependent molecular chaperone cochaperone-regulated conformational transitions hsp70-hsp90 multichaperone machine hsc70-driven clathrin uncoating large double-ring complexes fuzzy chaperone-substrate ensembles native low-energy conformations mitochondrial groel–groes system c-terminal ggap motif specialized cytosolic j-protein tpr domain-peptide complexes hsp70-hsp100-dependent disaggregation plastid development hsp70-hsp90 chaperone cascade personal data structure-based mutagenesis studies clathrin-coat disassembly illuminates protein triage decisions mammalian disaggregase machinery high-resolution solution structure hsc70/auxilin uncoating reaction coli σ32 protein
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headline:The Hsp70 chaperone network
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