Heat shock proteins research

This study shows that loss of GRPEL2 in mice protects against age- and diet-induced obesity and improves metabolic health without affecting mitochondrial protein import.

This study shows Hsp70 chaperones are essential for rhinovirus replication and identifies them as potential broad-spectrum antiviral targets.

This study shows azadiradione activates HSF1 by interacting with its DNA-binding domain, promoting oligomerization and HSE binding, independent of the oligomerization domain.

This study reveals that Hsp104, an AAA+ ATPase, functions as a bidirectional, processive translocase by switching direction through biased stochastic conformational transitions.

This study identifies Djp1 as a multifunctional Hsp40 cochaperone that regulates mitochondrial phospholipid metabolism through its interaction with Psd1 and independent roles.

This study identifies HAX1 as a stimulatory cofactor for CLPB, showing it promotes CLPB oligomerization and enhances its ATPase and refoldase activities.

The paper identifies FAM136A as a chaperone essential for mitochondrial membrane protein biogenesis, specifically for VDAC paralogs and some electron transport chain subunits.

The paper shows that electrostatic complementarity between ClpX's positively charged substrate-entry channel and substrate domains determines ATP-driven protein unfolding efficiency.

The paper examines the evolutionary divergence of the RAR1-SGT1 chaperone complex in leptosporangiate ferns, identifying key residues that dictate binding specificity and revealing a stepwise evolutionary pathway.

The paper shows that chaperone condensates specifically buffer the heat shock response, setting activation thresholds and ensuring specificity to heat shock in budding yeast.

This study uses single-molecule techniques to show how Hsp90 helps Hsp70 release folding intermediates and remodel client proteins to enable proper refolding.

The paper maps the TRiC/CCT interactome in mouse photoreceptors and identifies its role in energy metabolism and neurodegeneration.

This study identifies MSTO1 as a TRiC assembly factor, showing that its loss leads to reduced TRiC levels and mitochondrial dysfunction, linking cytosolic proteostasis to mitochondrial health.

The paper introduces nuclear PIMs to study nuclear quality control and shows that proteasome and VCP disaggregate nuclear aggregates, with subunits exported to the cytosol for aggrephagy.

This study defines DNAJA2 co-chaperone client selectivity using pulse-SILAC and BioID to reveal distinct protein pools associated with DNAJA2 based on structural and physicochemical properties.

The paper identifies dynamic acetylation changes in yeast during heat shock, showing acetylation regulates protein activity to enhance the heat shock response.

This study elucidates the TRiC-assisted folding of class I HDACs, revealing distinct co-chaperone and cofactor networks for HDAC1 and HDAC3, while HDAC8 folds independently.

This study shows that oxidation of Cys127 in Hsp42 promotes disulfide bond formation, oligomerization, and client selection in yeast under oxidative stress.

The paper identifies RPAP3 and PIH1D1 as R2TP subunits and shows their role in assembling INO80, SRCAP, and TIP60 complexes through physical interactions and functional validation.

This study identifies non-canonical mechanisms of HSP90C, a chloroplastic HSP90 chaperone, through structural and biophysical analyses, revealing features contributing to its high ATPase activity.

The paper evaluates Hsp60/10 client proteins in Alzheimer's disease, finding their decline correlates with proteostasis vulnerabilities, Braak/tau burden, and cognitive impairment.

This paper investigates how LonP1 protease uses ATP hydrolysis to regulate substrate translocation and proteolytic activation, showing that proteolysis of folded proteins requires ATP-driven unfolding and translocation.

This study shows heat stress activates UPRER through XBP-1 and HSF-1 in C. elegans, with cross-talk to cytosolic HSR and inter-tissue stress communication enhancing thermotolerance.

This study identifies Rqc1p as essential for yeast thermotolerance, showing it has nuclear localization signals and stable mRNA levels under heat shock.

This study investigates the conformational dynamics of the membrane-anchored foldase LipH and shows how it recognizes, folds, and releases its client lipase LipA.

This study investigates how Cys depletion in γD-crystallin leads to misfolding and aggregation through dimerization, revealing a novel pathway for age-related cataract formation.

The paper shows that chaperonin GroEL/S promotes drug resistance by recognizing protein dynamics, displacing inhibitors and restoring active enzyme function.

This study shows HOP forms stress-induced biomolecular condensates via phase separation driven by TPR domains, regulated by Hsp70 and Hsp90, and its dysfunction increases misfolding stress.

This study designs and characterizes de novo protein binders that specifically target the closed state of HSP90, showing their structural accuracy and functional properties.

This study shows that phosphorylation of Hsp70 enhances its ability to bind client proteins, improving its function in proteostasis across species.