Heat shock proteins research

The paper investigates the heat shock response in lymphoblastoid cell lines with and without trisomy 21, finding a more robust response in trisomy 21 cells.

The paper uses AlphaFold to predict the structure of sacsin's Hsp90-like domains and identifies key residues for ATPase activity, suggesting sacsin functions as an ATP-driven molecular chaperone.

The paper identifies subfunctionalized J-domain proteins in Arabidopsis thaliana that remodel protein aggregates, showing distinct stress responses and interactions with Hsp101.

The paper identifies a DNAJB4 variant causing chaperonopathy in skeletal muscle, leading to muscle weakness and specific pathological features in type 1 fibers.

This study uses NMR to show that the EEVD motif of HSP70 transiently binds multiple sites on Sis1, facilitating HSP70 interaction and client protein release.

The paper shows that mammalian cells can maintain critical Hsp90 levels through translational reprogramming in response to stress, ensuring viability despite genetic loss of Hsp90 alleles.

The paper identifies and characterizes HSP gene superfamily members in apple snails and analyzes their expression under temperature stress.

The paper identifies LarA as a regulator of Lon protease activation during proteotoxic stress, showing its role in modulating proteolysis through a specific C-terminal sequence.

This study identifies Hsc70 and Hsp70 as cellular proteins interacting with MVC viral proteins and shows their distinct roles in MVC infection, suggesting Hsp70 as a potential therapeutic target.

This study identifies the Plasmodium prefoldin complex as essential for proteotoxic stress response and demonstrates that biperiden inhibits its function, offering a new drug target for malaria.

This study identifies Asc1p and Hel2p as RQC factors that regulate HSP70 mRNA translation and degradation during heat stress and recovery in yeast.

The paper shows that ATP hydrolysis rates alter substrate specificity of the AAA+ protease ClpX, affecting its ability to degrade different substrates.

The paper defines and annotates 959 genes comprising the human proteostasis network, focusing on translation, protein folding, and organelle-specific systems.

The paper shows that budding yeast septins require chaperone assistance for native folding and complex assembly, with Cdc12 being highly dependent on chaperonins.

The paper shows that the C-terminal domain of Hsp70 paralogs Ssa3 and Ssa4 specifically regulates ribonucleotide reductase, affecting DNA damage resistance and RNR subunit stability.

The paper identifies transcellular chaperone signaling (TCS) as a gut-to-muscle stress response in C. elegans that bypasses HSF-1-mediated heat stress resistance.

This study reveals the structural and functional mechanism of CLPB, a mitochondrial AAA+ disaggregase, showing its unique assembly and substrate translocation properties.

This study uses a fluorescent reporter substrate to elucidate the stepwise mechanism of Hsp70 unfoldase action in converting aggregates into native proteins.

The paper shows that targeting ATM, ATR, or DNA topoisomerases causes widespread protein aggregation through chaperone system overload, similar to proteotoxic stress and proteinopathies.

The paper determines the cryo-EM structure of yeast Lon protease (PIM1) and shows it forms a hexamer similar to bacterial and human Lon proteases, with unique structural features and a dispensable yeast-specific insertion.

This study shows HSF1 and HSF2 regulate gene and enhancer transcription differently under oxidative stress and heat shock by controlling RNA polymerase II pause-release.

The paper investigates how mutations in UNC-45/UNC-45B affect myosin chaperone activity and protein stability in C. elegans, finding reduced chaperone activity and protein levels in most mutants.

This paper uses cross-linking mass spectrometry to characterize Hsp70 interactions in budding yeast, revealing self-association, multi-point client interactions, and novel PTMs critical for client function.

The paper develops a mouse model with a proteostasis reporter to study how cytoplasmic and nuclear protein aggregates affect neuronal protein quality control in aging and disease.

This study investigates the role of the R2TP chaperone in intestinal stem and progenitor cells, showing its critical function in proliferation and its association with poor colorectal cancer prognosis.

This study elucidates how McsB, a bacterial kinase, regulates protein degradation by switching between open and closed oligomer forms in response to stress.

This study shows that budding yeast adapts to long-term high temperature by reducing temperature-sensitive proteins, relocalizing the proteome, and altering protein conformations, which may confer new functions.

The paper identifies cytosolic chaperone interactions with a tumor-derived p53 mutant using split-YFP in budding yeast, showing temperature-sensitive nuclear exclusion and dominant-negative effects.

The paper introduces ReporterSeq, a method to identify genetic regulators of the heat shock response across diverse stressors and timepoints in budding yeast.