Hsp70 chaperones: cellular functions and molecular mechanism.
Matthias P. Mayer,Bernd Bukau +1 more
Reads0
Chats0
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
More filters
Journal ArticleDOI
Neuroprotective effects of increasing levels of HSP70 against neuroinflammation in Parkinson's disease model by inhibition of NF-κB and STAT3.
TL;DR: Findings indicate that supplementation with HSP70s recovered cell viability and MMP and reduced levels of ROS, apoptosis, and mitochondrial fragmentation.
Journal ArticleDOI
The cellular chaperone Hsc70 is specifically recruited to reovirus viral factories independently of its chaperone function.
TL;DR: The localization of the cellular chaperone Hsc70 is examined and it is found that it colocalizes with VFs in infected cells and also with viral factory-like structures (VFLs) formed by ectopically expressed μNS.
Journal ArticleDOI
Biochemical and biophysical characterization of small heat shock proteins from sugarcane. Involvement of a specific region located at the N-terminus with substrate specificity.
Ana O. Tiroli,Carlos H.I. Ramos +1 more
TL;DR: This is the first report on the chaperone activity of sugarcane small Hsps, and it is suggested that this specific region at the N-terminus is one of these sites involved with substrate specificity in smallHsps.
Journal ArticleDOI
Transcriptomic Analyses Reveal Novel Genes with Sexually Dimorphic Expression in Yellow Catfish ( Pelteobagrus fulvidraco ) Brain
Jianguo Lu,Jianguo Lu,Min Zheng,Min Zheng,Jiajia Zheng,Jian Liu,Yongzhuang Liu,Lina Peng,Lina Peng,Pingping Wang,Xiaofeng Zhang,Qiu-Shi Wang,Peixian Luan,Shahid Mahbooband,Xiaowen Sun +14 more
TL;DR: This work identifies a set of annotated genes that are candidate factors affecting sexual dimorphism as well as simple sequence repeat (SSR) and single nucleotide variation (SNV) in yellow catfish.
Journal ArticleDOI
Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s
TL;DR: Recent findings that suggest that despite their similarity, Ssa isoforms may have unique cellular functions are reviewed.
References
More filters
Journal ArticleDOI
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.