title: Unraveling the CHIP:Hsp70 complex as an information processor for protein quality control.
abstract: The CHIP:Hsp70 complex stands at the crossroads of the cellular protein quality control system. Hsp70 facilitates active refolding of misfolded client proteins, while CHIP directs ubiquitination of misfolded client proteins bound to Hsp70. The direct competition between CHIP and Hsp70 for the fate of misfolded proteins leads to the question: how does the CHIP:Hsp70 complex execute triage decisions that direct misfolded proteins for either refolding or degradation? The current body of literature points toward action of the CHIP:Hsp70 complex as an information processor that takes inputs in the form of client folding state, dynamics, and posttranslational modifications, then outputs either refolded or ubiquitinated client proteins. Herein we examine the CHIP:Hsp70 complex beginning with the structure and function of CHIP and Hsp70, followed by an examination of recent studies of the interactions and dynamics of the CHIP:Hsp70 complex.
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.
authors.forename: Jamie
authors.initials: J
authors.lastname: VanPelt
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA. Electronic address: pagerc@miamioh.edu.
authors.forename: Richard C
authors.initials: RC
authors.lastname: Page
mesh_terms: D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D017510:Protein Folding; D011499:Protein Processing, Post-Translational / Q000502:physiology; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination / Q000502:physiology
chemical_list: D018840:HSP70 Heat-Shock Proteins; D044767:Ubiquitin-Protein Ligases
keywords: Allostery; Dynamics; Protein quality control; Protein refolding; Ubiquitination