Hsp70 chaperones: Cellular functions and molecular mechanism

By M. Mayer, Bernd Bukau. Cellular and Molecular Life Sciences, 2005

2,912 citations recorded by the source corpus.

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.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d37ff8bf0fab9c3a53da161dfb22c5b3b151cb9b

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In Immunology

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Citations in the corpus

• Pathways of cellular proteostasis in aging and disease (2018, background): “Nucleotide exchange factors are necessary to allow Hsp70 to perform cycles of substrate binding and release (Laufen et al., 1999; Mayer and Bukau, 2005; Winkler et al., 2012).”
• Recent advances on Bayesian inference for $P(X < Y)$ (2011, background): “Moreover, it is known that the presence of the Hsp70 protein can induce the development of pathological states, such as oncogenesis (see Mayer and Bukau, 2005), and that seems to limit the efficacy of the chemotherapy treatment in diseased patients.”
• Combined drought and heat stress in wheat: changes in some heat shock proteins (2011, background): “Some members of this family are expressed constitutively, while others are expressed during environmental stresses and are involved in refolding of non-native proteins (Vierling 1991, Miernyk 1999, Wang et al. 2004, Mayer et al. 2005).”
• The heat shock response: life on the verge of death. (2010, background): “Under physiological conditions, Hsp70s are involved in the de novo folding of proteins, and under stress they prevent the aggregation of unfolding proteins and can even refold aggregated proteins (Mayer and Bukau, 2005).”
• The Hsp70 chaperone machinery: J-proteins as drivers of functional specificity (2010, neutral): “The 40 kDa amino-terminal adenine nucleotide-binding domain regulates the conformation of the 25 kDa carboxy-terminal peptide-binding domain (PBD), which binds to a five amino acid segment of clients that is enriched in hydrophobic residue”
• What are you actually measuring? A review of techniques that integrate the stress response on distinct time‐scales (2020, background): “Heat shock proteins (Hsp) play crucial roles in maintaining proper protein folding and protecting cells against stress (Li & Srivastava, 2003) and are also associated with Cort receptor signal transduction (Mayer & Bukau, 2005).”
• Role of Heat Shock Proteins in Livestock Adaptation to Heat Stress (2017, background): “ATP binding and hydrolysis are necessary for the chaperonic activity of HSPs where 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 will control the ATPase cycle ”