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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Stress-induced HSP70 from Musca domestica plays a functionally significant role in the immune system
TL;DR: Results showed high mortality in larvae treated with dsRNA of MdHSP70 at heat shock, Cd stress and bacterial invasion, suggesting that MdH SP70 is potentially involved in the stress and immune responses of the house fly and perhaps contributes to protection against cellular injury.
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Recent advances on Bayesian inference for $P(X < Y)$
Laura Ventura,Walter Racugno +1 more
TL;DR: In this article, the authors proposed a matching prior based on higher-order asymptotics and pseudo-likelihoods, which allows one to perform accurate inference on the parameter of interest $R$ only, even for small sample sizes.
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Immunotherapy of Radioresistant Mammary Tumors with Early Metastasis Using Molecular Chaperone Vaccines Combined with Ionizing Radiation
TL;DR: Results indicate that Hsp70.PC-F vaccine can induce specific immunity to radioresistant populations of mammary tumor cells and, thus, can complement radiotherapy, leading to synergistic killing.
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Therapeutic potential of heat shock protein induction for muscular dystrophy and other muscle wasting conditions.
TL;DR: Evidence supporting HSP induction for muscular dystrophy and other muscle wasting conditions is provided, including sarcopenia, cancer cachexia, sepsis, denervation, burns, and chronic obstructive pulmonary disease.
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MiR-30c: A novel regulator of salt tolerance in tilapia
TL;DR: It is revealed that miR-30c, a kidney-enriched miRNA, emerges as a crucial osmoregulator in Nile tilapia and may be developed as a molecular marker to assist to breed or genetically engineer salt tolerant species.
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.