ReviewCell stress & chaperones2020
Peeking from behind the veil of enigma: emerging insights on small heat shock protein structure and function.
Review in Cell stress & chaperones, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- Disorder with consequence: Phosphorylation sites in HSPB5 yield distinct structural outcomes.bioRxiv : the preprint server for biology · 2025Article
- Small heat shock protein HSPB5 uses disorder to bind zinc with high affinity.bioRxiv : the preprint server for biology · 2025Article
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- How does protein aggregate structure affect mechanisms of disaggregation?Biochemical Society transactions · 2025Review
- Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Capturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution.Journal of the American Chemical Society · 2025Article
- Article
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.Nature communications · 2024Article
- High-Performance Workflow for Identifying Site-Specific Crosslinks Originating from a Genetically Incorporated, Photoreactive Amino Acid.Journal of proteome research · 2024Article
- The α-crystallin Chaperones Undergo a Quasi-ordered Co-aggregation Process in Response to Saturating Client Interaction.Journal of molecular biology · 2024Article
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.bioRxiv : the preprint server for biology · 2024Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
- HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.International journal of molecular sciences · 2023Article
- A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli.Cell stress & chaperones · 2023Review
- Site-Specific Glycation of Human Heat Shock Protein (Hsp27) Enhances Its Chaperone Activity.ACS chemical biology · 2023Article
- HSPB8 frameshift mutant aggregates weaken chaperone-assisted selective autophagy in neuromyopathies.Autophagy · 2023Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved.The Journal of cell biology · 2022Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
This is a short paper on new ways to think about the structure and function of small heat shock proteins (sHSPs), perhaps the most enigmatic family among protein chaperones. The goal is to incorporate new observations regarding the disordered regions of small heat shock proteins (sHSPs) into the large body of structural information on the conserved structural alpha-crystallin domains (ACD) that define the sHSP family. Disordered regions (N-terminal region and C-terminal region or NTR and CTR, respectively) represent over 50% of the sHSP sequence space in the human genome and are refractory to traditional structural biology approaches, posing a roadblock on the path towards a mechanistic understanding of how sHSPs function. A model in which an ACD dimer serves as a template that presents three grooves into which other proteins or other segments of sHSPs can bind is presented. Short segments within the disordered regions are observed to bind into the ACD grooves. There are more binding segments than there are grooves, and each binding event is weak and transient, creating a dynamic equilibrium of tethered and untethered disordered regions. The ability of an NTR to be in dynamic equilibrium between tethered/sequestered and untethered states suggests several mechanistic alternatives that need not be mutually exclusive. New ways of thinking about (and approaching) the intrinsic properties of sHSPs may finally allow the veil of enigma to be removed from sHSPs.
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