Heat shock proteins research

GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome

This study investigates how GroEL/ES interacts with nascent proteins on ribosomes, showing that GroEL binds and destabilizes substrates, while GroES facilitates partial encapsulation and refolding.

Stress granules and protein aggregates reveal intracellular resource competition

This study shows that competition for molecular chaperones limits stress granule disassembly, leading to their persistence and solidification, potentially contributing to neurodegenerative diseases.

Requirement of ClpX for CtsR dissociation from its operator elements upon heat stress in Bacillus subtilis

This study shows that ClpX is required for CtsR dissociation from its operator elements during heat stress in Bacillus subtilis, highlighting its role in activating the stress response regulon.

Distinct modes of redox-mediated DegP activation govern its role as a general protease

This study identifies two distinct redox-mediated mechanisms that activate DegP, a protease in E. coli, enabling it to function as a general protease under various stress conditions.

The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices.

This study characterizes the conformational preferences of C-terminal tails in GroEL, mHsp60, and Cpn60 using spectroscopy, revealing they adopt polyproline II helices rather than being fully disordered.

Deep conservation of mitochondrial HSP60 structure with lineage-specific and context-dependent regulation reflects thermal resilience in cnidarians

This study compares HSP60 expression in three cnidarians under thermal stress, revealing lineage-specific regulation and deep evolutionary conservation of the chaperonin.

Disorder with consequence: Phosphorylation sites in HSPB5 yield distinct structural outcomes

This study examines how phosphorylation at different sites in HSPB5 affects its oligomeric structure and function, revealing distinct cellular outcomes based on the extent of phosphorylation.

Structure of ER chaperone complex GRP170-ATP-BiP suggests a new model for substrate engagement

The paper reports the cryo-EM structure of the GRP170-ATP-BiP complex, revealing a new model for substrate engagement and GRP170's pseudo-ATPase activity.

A default silencing mechanism restrains stress-induced genes in C. elegans

The paper identifies ZNF-236 as a key factor maintaining quiescence of stress-induced genes in C. elegans, showing that this silencing is an active genomic state, not passive.

Collaboration between two conserved sequence motifs drives ATPase stimulation of Hsp90 by Aha1

This study shows how two conserved motifs in Aha1 regulate Hsp90 ATPase activity and client protein folding by interacting structurally and functionally.

Conserved intrinsically disordered region of DNAJB6 dictates its surveillance of FG-Nup condensates

The paper shows that DNAJB6's conserved intrinsically disordered region enables its surveillance of FG-Nup condensates by forming stable assemblies that outcompete FG-Nup interactions.

Tryptoline Stereoprobe Elaboration Identifies Inhibitors of the GRPEL1-HSPA9 Chaperone Complex

The paper identifies inhibitors of the GRPEL1-HSPA9 chaperone complex using tryptoline stereoprobes and shows they target non-orthosteric sites.

Structural basis for the folding of PINK1 by the HSP90-CDC37 chaperone complex

This study presents the cryo-EM structure of the PINK1-HSP90-CDC37 complex, revealing how HSP90-CDC37 stabilizes PINK1 and how mutations may disrupt this process.

Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP

The paper presents the cryo-EM structure of the MecA/ClpC/ClpP complex from Staphylococcus aureus, revealing how MecA facilitates substrate transfer and how ClpC/ClpP interactions are regulated by ATPase activity.

Cellular moonlighting function of Hsp20 directs morphological and pathogenic development in Ustilago maydis

This study shows that Hsp20 in Ustilago maydis forms punctate structures that sequester proteins like actin and septin, affecting pathogenicity and cellular processes.

Comparative analysis of hsp16 and hsp70 heat shock protein families in Caenorhabditis nematodes

This study compares hsp16 and hsp70 heat shock protein families in Caenorhabditis nematodes, revealing differences in evolutionary conservation, genomic organization, and expression patterns between species.

CHIP, VCP, and Nucleolar Gatekeepers Remodel the Nucleolus into a Stress-Responsive Proteostasis Hub

This paper shows that the nucleolus becomes a stress-responsive proteostasis hub during heat shock, regulated by CHIP, VCP, and gatekeepers like NOL6 and WDR55.

Structural basis for ATP-driven double-ring assembly of the human mitochondrial Hsp60 chaperonin

The paper presents cryo-EM structures of human mitochondrial Hsp60 chaperonin in different states to elucidate the structural basis of ATP-driven double-ring assembly.

Nuclear and cytosolic J-domain proteins provide synergistic control of Hsf1 at distinct phases of the heat shock response

This study identifies Apj1 and Ydj1 as J-domain proteins that regulate Hsf1 in distinct phases of the heat shock response in yeast.

Maintaining the methionine residues of the chaperone Spy in a reduced state is crucial for periplasmic proteostasis.

This study shows that chlorite stress increases Spy production, and MsrPQ repairs oxidized Spy to maintain periplasmic protein homeostasis.

Single particle dynamics of protein aggregation and disaggregation in the presence of the sHsp proteins IbpAB

This study uses Burst Analysis Spectroscopy to show IbpAB alters aggregate structure, enabling efficient disaggregation by KJEB, independent of particle size.

Impact of sex and glial tau expression on heat shock protein induction in a Drosophila model of tauopathy

This study examines how sex and glial tau expression affect heat shock protein induction in a Drosophila tauopathy model, finding sexually dimorphic Hsp expression and tau-induced disruption of Hsp induction.

DnaK refolds denatured proteins by actively pulling out their misfolded structural elements

This paper uses AlphaFold3 and molecular dynamics simulations to reveal how DnaK refolds denatured proteins by actively extracting misfolded helices through ATP-driven lid movement.

A widespread protein misfolding mechanism is differentially rescued by chaperones based on gene essentiality

The paper identifies a widespread protein misfolding mechanism involving non-covalent lasso entanglement (NCLE) and shows that chaperones rescue it more effectively for essential proteins.

Profiling the physiological impact of aberrant folded-state protein filamentation in cells

This study investigates the physiological impact of folded-state protein agglomerates in yeast, finding they do not disrupt proteostasis or cell fitness and show minimal effects on cellular processes.

Competing chaperone pathways in α-synuclein disaggregation and aggregation dynamics

This study investigates the interaction between sHsps and Hsp70 chaperones in α-synuclein disaggregation and aggregation, finding no synergy and potential antagonism between the chaperone classes.

Declining intracellular proteostasis capacity drives misfolded protein secretion in senescent human cells.

This study shows that senescent human cells secrete misfolded proteins via the endo-lysosomal system, driven by DNAJC5 and reduced intracellular proteostasis.

Cryo-EM Reveals Regulatory Mechanisms Governing Substrate Selection and Activation of Human LONP1

This study uses cryo-EM to identify a novel intermediate state of LONP1 that regulates substrate selection and activation, providing insights into its role in mitochondrial proteostasis.

Hsp70 is phosphorylated in a conserved response to DNA damage and contributes to cell cycle control

The paper shows that Hsp70 phosphorylation at T495 occurs in human cells during DNA damage and affects cell cycle control, with similar effects observed in yeast.

Visualizing nucleation, condensation and propagation of β-tubulin folding in chaperonin TRiC

The paper visualizes the nucleation, condensation, and propagation of β-tubulin folding in the chaperonin TRiC, showing a hierarchical process involving nonnative structures and TRiC subunits.