Heat shock proteins research

This paper identifies a mitochondrial insertion in ClpX that facilitates substrate recruitment and processing, with distinct roles in yeast and human systems.

This study shows that HSF1 forms stress-induced condensates with divergent transcriptional outcomes, impacting transcriptional responses during different stress conditions.

This study examines how Class B J-Domain Proteins enhance Hsp70-mediated protein disaggregation through autoinhibition and EEVD motif interactions.

The paper identifies BAG6 and RNF126 as key players in PQC degradation of non-native missense protein variants using CRISPR screens and VAMP-seq.

This study shows that inhibiting Hsp70 reduces chikungunya virus infectious particle production without harming host cells.

This study investigates how LCA-linked mutations in TRiC/CCT subunit CCT2 disrupt its allosteric network and functional cycle, leading to structural and functional defects associated with Leber Congenital Amaurosis.

The paper identifies and characterizes HSP70 family members in the Cuban painted snail Polymita picta to assess their role in thermoresistance and adaptation to climate change.

This study presents the first crystal structure of HtpGMtb, revealing a conformationally silent dimer and direct TLR4 interaction, providing insights into its catalytic activity and TLR4 activation mechanism.

This study uses computational methods to predict and analyze ClpK protein interactions in Klebsiella pneumoniae, identifying KPN_01323 as a promising interaction partner.

This study reveals the structural mechanism of McsAB-mediated suppression of CtsR during heat shock, showing autophosphorylation is essential for rapid response.

This study investigates the role of Hsp110 in Drosophila, showing its essential and dosage-sensitive function in nervous system development and survival.

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

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.

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

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.

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.

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.

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.

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

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.

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.

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.

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.

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.

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.

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

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.

This study investigates the function of CDJ5 in Chlamydomonas reinhardtii by comparing its proxiomes with and without a functional 4Fe-4S cluster, revealing its role in chloroplast microcompartment localization and photosynthetic processes.

The paper identifies Arg80 as a key regulator of proteostasis in S. cerevisiae, showing its role in mitigating proteotoxic stress through interactions with arginine metabolism and stress response pathways.

This study shows chaperones modulate enzyme activity in native states, expanding their role beyond protein folding.