Aug 2026· microPublication Biology· Vol 2026· 0 citations· 17 references
Medicine
TL;DR
Comparative analyses reveal substantial diversity in tissue expression, intrinsic disorder, and liquid-liquid phase separation (LLPS) propensity, highlighting extensive functional specialization within the C. elegans sHSP family.
Abstract
Small heat shock proteins (sHSPs) are ATP-independent molecular chaperones with diverse cellular functions. Here, we systematically reassessed two subfamilies of sHSPs in C. elegans by integrating evolutionary, genomic, and biophysical analyses. We report analysis of 18 α-crystallin domain-containing sHSPs, including two previously uncharacterized HSP-16-like proteins (designated hsp-16.31 & hsp-16.32 ). This analysis also supports the inclusion of two other proteins, ZK1128.7 and Y55F3BR.6 , as additional members of the C. elegans sHSP family. Comparative analyses reveal substantial diversity in tissue expression, intrinsic disorder, and liquid-liquid phase separation (LLPS) propensity, highlighting extensive functional specialization within the family.
A genome-wide analysis of the HSP gene family is performed to provide a genomic framework for HSP genes in L. vannamei and identify candidate genes and variants associated with thermal stress responses.
Aminah A. Barqawi· Comparative Biochemistry and...· 0 citations
A genome-wide identification and comparative analysis of the CSP gene family in yak is performed primarily using bioinformatics approaches based on publicly available genomic and transcriptomic datasets, along with a preliminary validation of their differential expression under cold and hypoxic stress.
These findings reconstruct the evolutionary emergence of the DGF-1 architecture from pre-existing structural modules and provide a framework for one of the largest and most enigmatic gene families in trypanosomatids.
Mathias J. Mangino, Juan Manuel Trinidad-Barnech, A. Parodi-Talice et al.· bioRxiv· 0 citations
The Thanatos-associated (THAP) protein family, named after the Greek god of death, comprises zinc-finger proteins characterized by a DNA-binding domain called the THAP domain. Although THAP1 and THAP11 have been extensively studied, the broader family of twelve human THAP-domain containing proteins is increasingly recognized as an important but underexplored group of transcriptional regulators. Evidence now links THAP proteins to a wide range of cellular processes, including cell-cycle progression, DNA repair, apoptosis, proteostasis, and mitochondrial function. Dysregulation of these proteins has also been implicated in cancer and neurological disorders, underscoring their medical relevance. In this review, we summarize current knowledge of their structure, localization, transcriptional roles, and disease associations. We also present new structural analyses that shed light on conserved and divergent features across the THAP family. Finally, we will highlight their newly appreciated functions in stem and progenitor cell biology.
B. Rampal, Alexandre Brisson, Louise Ben Hamou Kuijpers et al.· Cellular and Molecular Life...· 0 citations
An evolved hierarchy of paralog-specific JDP couplings that dynamically rewires the Hsp70 network from active repair to protection during stress is revealed, revealing an evolved hierarchy of paralog-specific JDP couplings that dynamically rewires the Hsp70 network from active repair to protection during stress.
Roni Suhler, Lars J. W. van Beurden, Merav D. Shmueli et al.· Proceedings of the National...· 0 citations
Heat shock cognate protein 70 (Hsc70) is a 71 kDa molecular chaperone belonging to the Hsp70 family of heat shock proteins. These proteins act as ATP-dependent molecular machines that assist protein folding under both physiological and stress conditions such as hypoxia, heat shock, and pH fluctuations. In addition to general chaperone functions, Hsc70 performs specialized roles, including uncoating clathrin-coated vesicles, facilitating protein transport into organelles, and targeting proteins for lysosomal degradation. Members of the Hsp70 family are known to form dimers and higher oligomers, but the structural organization and functional relevance of these assemblies remain poorly understood. Earlier studies also suggested that J-domain proteins (JDPs) can promote Hsp70 dimerization. In this study, we used chemical cross-linking, high-resolution Fourier transform mass spectrometry (FTMS), 15N isotopic labeling, and advanced data analysis to investigate the structural organization of Hsc70 dimers. Cross-link-derived distance restraints enabled structural modeling of Hsc70 monomers and dimers using AlphaLink2. Our results reveal distinct ATP- and ADP-state dimer conformations that coexist in equilibrium. In the presence of the cochaperone DnaJB1, we observed a shift in the dimer–monomer equilibrium, accompanied by enhanced ATP hydrolysis and formation of intermediate species. These findings demonstrate that the Hsc70 dimer population is structurally heterogeneous and depends on nucleotide state and cochaperone interactions.
A. Melikov, Vsevolod Viliuga, Daniel Kavan et al.· Journal of Proteome Research· 0 citations