Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates |
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Authors: | Chamithi Karunanayake Richard C Page |
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Affiliation: | Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA |
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Abstract: | The chaperone heat shock protein 70 (Hsp70) and its network of co-chaperones serve as a central hub of cellular protein quality control mechanisms. Domain organization in Hsp70 dictates ATPase activity, ATP dependent allosteric regulation, client/substrate binding and release, and interactions with co-chaperones. The protein quality control activities of Hsp70 are classified as foldase, holdase, and disaggregase activities. Co-chaperones directly assisting protein refolding included J domain proteins and nucleotide exchange factors. However, co-chaperones can also be grouped and explored based on which domain of Hsp70 they interact. Here we discuss how the network of cytosolic co-chaperones for Hsp70 contributes to the functions of Hsp70 while closely looking at their structural features. Comparison of domain organization and the structures of co-chaperones enables greater understanding of the interactions, mechanisms of action, and roles played in protein quality control. |
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Keywords: | Hsp70 molecular chaperones co-chaperones protein quality control J domain protein nucleotide exchange factor Hsp40 GrpE BAG Hsp110 CHIP SMADs Hop Hip Hsp90 |
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