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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Use of Different Cooling Methods in Pig Facilities to Alleviate the Effects of Heat Stress-A Review
TL;DR: The effectiveness of cooling technologies in pig facilities is discussed, taking into consideration the indicators of animal welfare such as respiratory rate, skin surface and body core temperature, performance parameters and behavioural changes.
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Non-canonical Interactions between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release
TL;DR: The results suggest that Bag1 and Bag3 control the stability of the Hsc70-client complex using at least two distinct protein-protein contacts, providing a previously under-appreciated layer of molecular regulation in the human H scsc70 system.
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Proteome-wide identification of HSP70/HSC70 chaperone clients in human cells.
Seung Woo Ryu,Rose Stewart,D Chase Pectol,Nicolette A. Ender,Oshadi Wimalarathne,Ji-Hoon Lee,Carlos P. Zanini,Antony Harvey,Jon M. Huibregtse,Peter R. Mueller,Tanya T. Paull +10 more
TL;DR: Together these findings show that the ubiquitin-activated interaction trap (UBAIT) fusion system can efficiently isolate the complex interactome of HSP chaperone family proteins under normal and stress conditions.
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Transcriptome sequencing and comparative analysis of the gametophyte thalli of Pyropia tenera under normal and high temperature conditions
San Choi,Mi Sook Hwang,Sungoh Im,Namju Kim,Won-Joong Jeong,Eun-Jeong Park,Yong-Gun Gong,Dong-Woog Choi +7 more
TL;DR: A comparison of the ESTs from gametophyte thalli under normal and heat stress conditions enabled us to identify the transcripts that were up or downregulated by high temperature, and most of transcripts produced under the high temperature condition belong to heat shock protein family and novel transcripts not matched to known genes in current public databases.
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Bioenergetics profile of CD4(+) T cells in relapsing remitting multiple sclerosis subjects.
Lidia De Riccardis,Antonia Rizzello,Alessandra Ferramosca,Emanuela Urso,Francesca De Robertis,Antonio Danieli,Anna Maria Giudetti,Giorgio Trianni,Vincenzo Zara,Michele Maffia +9 more
TL;DR: This work focused on the metabolic reprogramming of CD4(+) T cells in MS subjects, paying attention to mitochondrial function and response to oxidative stress.
References
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Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
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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Hsp90 as a capacitor for morphological evolution
TL;DR: It is reported that when Drosophila Hsp90 is mutant or pharmacologically impaired, phenotypic variation affecting nearly any adult structure is produced, with specific variants depending on the genetic background and occurring both in laboratory strains and in wild populations.
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Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
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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Invited Review: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance
TL;DR: Recent evidence and hypotheses suggesting that the HSPs may be important modifying factors in cellular responses to a variety of physiologically relevant conditions such as hyperthermia, exercise, oxidative stress, metabolic challenge, and aging are examined.
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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.