Protein Disaggregation by Hsp70 Chaperone System

Description

This lecture by the instructor covers the role of the Hsp70 chaperone system in controlling protein disaggregation and refolding. It discusses how Hsp70, Hsp40, and Hsp104 chaperones work together to modify aggregates, bind to aggregates, and activate disaggregation, ultimately leading to protein refolding. The lecture also explores the significance of aggregate modification for protein disaggregation and the different modes of Ssa1 recruitment to aggregates driven by Sis1 and Ydj1. Additionally, it delves into the interaction between Sis1 and Hsp70's EEVD-motif in aggregate remodeling. Various experiments and models are presented to illustrate the mechanisms and outcomes of protein disaggregation by the Hsp70 chaperone system.

Official source

https://mediaspace.epfl.ch/media/0_qzbfuowm

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In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state.

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In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA.

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Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress.

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Adenosine triphosphate

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