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The Chaperone Networks: A Heat Shock Protein (Hsp)70 Perspective

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The Molecular Chaperones Interaction Networks in Protein Folding and Degradation

Part of the book series: Interactomics and Systems Biology ((INTERACTOM,volume 1))

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Abstract

The heat shock protein (Hsp)70 protein chaperone is a ubiquitous and promiscuous simple machine that functions in a wide variety of cellular processes. Its primary role of binding short, exposed hydrophobic stretches in misfolded polypeptides is augmented by the participation of an array of partners that act at multiple levels to govern Hsp70 functionality. Protein folding by Hsp70 is adenosine triphosphate (ATP)-dependent and the state of nucleotide binding is driven by dedicated Hsp70 cofactors. Moreover, these and other associates provide functional specificity by virtue of pathway-specific interactions that both recruit and regulate Hsp70 to provide critical protein remodeling contributions. In this chapter, we break down these interactions into two broad themes: protein biogenesis and maturation, and quality control surveillance and degradation. Key findings that establish the pathway- or process-specific network around Hsp70 supporting each cellular activity are discussed, with special attention paid to protein interactions that dictate the contextual role Hsp70 plays. Understanding these various chaperone networks is a requisite first step in designing pathway-specific pharmacological agents for potential therapeutic intervention in protein misfolding disorders.

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    Veronica M. Garcia & Prof. Kevin A. Morano PhD

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    Walid A. Houry

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Garcia, V., Morano, K. (2014). The Chaperone Networks: A Heat Shock Protein (Hsp)70 Perspective. In: Houry, W. (eds) The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Interactomics and Systems Biology, vol 1. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1130-1_4

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