Open AccessCytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates
Author(s) -
Chamithi Karunanayake,
Richard C. Page
Publication year - 2021
Publication title -
experimental biology and medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.012
H-Index - 146
eISSN - 1535-3702
pISSN - 1535-3699
DOI - 10.1177/1535370221999812
Subject(s) - chaperone (clinical) , co chaperone , allosteric regulation , hsp70 , cytosol , microbiology and biotechnology , protein folding , biology , foldase , proteostasis , hsp90 , heat shock protein , biochemistry , enzyme , groel , medicine , pathology , escherichia coli , gene
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.