Heat shock proteins research

Loss of mitochondrial co-chaperone GRPEL2 protects mice from age- and diet-induced obesity

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.

The heat shock protein 70 (Hsp70) family of chaperones is essential for rhinovirus replication

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

Azadiradione regulates Heat Shock Factor 1 function by interacting with its DNA-binding domain independent of the oligomerization domain

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

Biased stochastic motor dynamics drive bidirectional, processive translocation by the AAA+ disaggregase Hsp104.

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

Djp1 is a multifunctional Hsp40 cochaperone for mitochondrial phospholipid metabolism

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

HAX1 drives assembly and activation of the mitochondrial intermembrane space chaperone CLPB

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

FAM136A is an essential chaperone for mitochondrial membrane protein biogenesis

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

Electrostatic Complementarity at the ClpX Substrate-EntryChannel Governs ATP-Driven Protein Unfolding

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

Stepwise and lineage-specific divergence of a major immune co-chaperone complex in leptosporangiate ferns

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.

Chaperone condensates buffer the heat shock response against pleiotropic inputs

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

Direct single-molecule visualization of Hsp90-mediated relief of a Hsp70-folding block

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

Mapping the chaperonin TRiC/CCT interactome in mouse photoreceptors reveals functional significance for energy metabolism

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

MSTO1 functions as a TRiC assembly factor linking cytosolic proteostasis to mitochondrial function

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.

Rapid removal of nuclear aggregates via proteasome- and VCP-dependent disaggregation

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.

Chaperoning through time - defining DNAJA2 co-chaperone client selectivity via pulse-SILAC and BioID.

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.

Dynamic global acetylation remodeling during the yeast heat shock response

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

TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks

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.

Intermolecular disulfide bond formation promotes Hsp42 higher-order assembly and shapes client selection in yeast

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

A large-scale analysis of the R2TP chaperone network reveals its contribution to the assembly of INO80, SRCAP and TIP60

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.

Structural basis of HSP90C, a highly active chloroplastic HSP90 chaperone from A. thaliana

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.

Mitochondrial Hsp60/10 Client Protein Decline Reveals Braak/Tau- and Cognition-Linked Proteostasis Vulnerabilities in Alzheimer's Disease

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

Mitochondrial Lon protease couples substrate translocation to proteolytic activation

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.

A non-canonical role for UPRER during heat stress in C. elegans.

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.

Structural and functional insights into yeast Rqc1p, a protein required for thermotolerance with potential nuclear localization

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

Conformational dynamics of the membrane-anchored foldase LipH from Pseudomonas aeruginosa governs recognition and release of its client lipase

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

Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin

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.

Chaperonin recognition of protein dynamics drives drug resistance

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

TPR Domains Drive the Functional Phase Separation of HOP and its Regulation by Hsp90 and Hsp70

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.

Structural analysis of de novo designed binders targeting the closed state of HSP90

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

Phosphorylation-dependent regulation of Hsp70 chaperones stimulates client recruitment

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