Heat shock proteins research

The paper presents a cryo-EM structure of a ClpXP-substrate complex, revealing an intermediate state in protein unfolding by the AAA+ proteolytic machine.

This study shows ADP-bound mtHSP70 binds preferentially to GRPEL1 over GRPEL2, with structural insights into their functional differences.

This study uses MD simulations and machine learning to reveal a two-stage binding mechanism of Hsp90 inhibitor Geldanamycin, showing stabilization of the loop-out conformation and involvement of both conformational selection and induced fit.

This study shows that HSP101 stabilizes HSA32, an aggregation-prone protein, which is essential for maintaining heat acclimation memory in Arabidopsis.

The paper identifies DivIVA and Mbl as substrates of the ClpYQ protease in Bacillus subtilis, showing their degradation in vitro and in vivo.

This study uses single-molecule nanopore experiments to demonstrate Hsp70 chaperones exert forces equivalent to 46 pN to extract trapped polypeptides, supporting the Entropic Pulling mechanism.

This study identifies S-HsfA2 in Arabidopsis as a factor that prevents hyperactivation of the heat stress response, balancing heat resistance and growth.

This study shows that in aging mouse hearts, Unc45b and Hsp70 levels decline at the protein level, while Hsp90 remains stable, potentially contributing to age-related cardiomyopathies.

The paper disrupts each gene in the yeast heat shock response to identify feedback loops regulating Hsp70 expression and localization, revealing spatiotemporal control mechanisms.

The paper identifies that reducing mitochondrial protein import capacity alleviates cytosolic protein misfolding fitness defects in yeast by enhancing proteostasis.

This study investigates how HSP60 deficiency disrupts mitochondrial proteostasis and dysregulates cholesterol synthesis, leading to developmental abnormalities and hypomyelination.

This study shows that HOP stabilizes HSFA1a in Arabidopsis, which is required for the heat stress response during thermomorphogenesis.

This study shows TRC40 switches from an ATP-dependent targeting factor to an ATP-independent chaperone under oxidative stress, preventing protein aggregation and supporting proteostasis.

This study uses a single turnover stopped-flow fluorescence method to show ClpB catalyzes processive protein unfolding at ~0.9 aa/s with a step-size of ~60 amino acids.

This study shows that loss of zebrafish Ba-crystallin (cryaba) increases age-related cataract, while loss of A-crystallin (cryaa) does not, highlighting an ontogenetic shift in crystallin function during lens development.

This study investigates the functional mechanisms of Hsp60 in Sulfolobus acidocaldarius, revealing its role in protein folding and membrane protection under stress.

This study investigates how phosphorylation of tyrosine residues in human Hsp90 affects its interactions with cochaperones and clients using yeast and cell-based assays.

This study redefines the hand-over-hand translocation mechanism of LONP1 using cryo-EM structures and biochemical assays, showing substrate binding regulates activity and ADP-bound ATPases can support translocation.

The paper investigates how chaperones coordinate during cotranslational protein folding in bacteria, showing they create a protected space for maturation without destabilizing intermediates.

This study shows that knocking out six Hsp70 genes in Drosophila reduces locomotor speed and disrupts adaptation to exercise training, with changes in leg muscle gene expression.

The paper shows mitochondrial thermogenesis generates heat that triggers a nuclear heat-shock response in mammalian cells.

This study identifies indole-containing compounds that disrupt HSP90-HIF1α interactions by binding to the C-terminal ATP site, showing potential for repurposing tryptamine derivatives to treat hypoxic tumors.

The paper develops a fluorescence-based sensor to measure protein kinase stability in live cells and shows its utility in studying oncogenic mutations and HSP90 chaperone effects.

This study shows that loss of HSF1 in MPNST cells causes proteomic imbalance and tumor suppression by inducing proteomic catastrophe through amyloidogenesis and mTORC1 inhibition.

This study shows that CUL-6 ubiquitin ligase promotes thermotolerance by degrading HSP-90 in intestinal lysosomes, independent of HSF-1.

This study shows that 3xGFP overproduction causes cytotoxicity through degradation overload, not aggregate formation, as it traps Hsp70 and disrupts the ubiquitin-proteasome system.

The paper shows that eukaryotic Hsp60/10 systems with dicarboxylic acids mimic GroEL/ES activity in vitro, altering the folding landscape specifically for eukaryotic chaperonins.

The paper uses qXL-MS to study interactome changes during heat stress, finding RNA-binding proteins show significant interactome shifts, suggesting RNA acts as a temperature sensor.

This study identifies the role of Ranbp2's cyclophilin domain in regulating crystallin proteostasis and neuroprotection in the chorioretina through proteomic analysis of genetically modified mice.

The paper investigates how J-domain proteins in yeast regulate Hsp70 chaperones through intramolecular interactions, showing auto-regulatory effects that reduce ATPase cycles.