ReviewCell stress & chaperones2002
Actin cytoskeleton and small heat shock proteins: how do they interact?
Review in Cell stress & chaperones, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
136 citing papers in PubMed.
- HSP60 and HSP10 depletion provoke distinct biological responses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Article
- Identification and characterization of the HSP gene family in the Chinese giant salamander: Expression patterns under combined environmental stress.BMC genomics · 2026Article
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Testicular Heat-Shock Protein Expression in Rats Following 3.5 GHz and 24 GHz RF-EMF Exposure.International journal of molecular sciences · 2026Article
- The Role of Thermal Immunomodulation in Postoperative Wound Repair with a Focus on Hepatic Surgery.International journal of molecular sciences · 2026Review
- Review
- RNA-seq reveals changes in the transcriptome of the breast muscle of adult female chickens in response to heat stress.BMC genomics · 2024Article
- Review
- Conserved mechanisms of self-renewal and pluripotency in mouse and human ESCs regulated by simulated microgravity using a 3D clinostat.Cell death discovery · 2024Article
- Resolution of inflammation in chronic disease via restoration of the heat shock response (HSR).Cell stress & chaperones · 2024Review
- The role of molecular chaperones in the mechanisms of epileptogenesis.Cell stress & chaperones · 2023Review
- Time-Course and Tissue-Specific Molecular Responses to Acute Thermal Stress in Japanese Mantis ShrimpInternational journal of molecular sciences · 2023Article
- Impact of Non-Invasive Physical Plasma on Heat Shock Protein Functionality in Eukaryotic Cells.Biomedicines · 2023Article
- Contribution of Extracellular Vesicles and Molecular Chaperones in Age-Related Neurodegenerative Disorders of the CNS.International journal of molecular sciences · 2023Review
- The lysophosphatidic acid-regulated signal transduction network in ovarian cancer cells and its role in actomyosin dynamics, cell migration and entosis.Theranostics · 2023Article
- Peptains block retinal ganglion cell death in animal models of ocular hypertension: implications for neuroprotection in glaucoma.Cell death & disease · 2022Article
- Article
- Molecular Mechanism Based on Histopathology, Antioxidant System and Transcriptomic Profiles in Heat Stress Response in the Gills of Japanese Flounder.International journal of molecular sciences · 2022Article
- Insights into the Mechanisms of Heat Priming and Thermotolerance in Tobacco Pollen.International journal of molecular sciences · 2021Article
- Alantolactone suppresses the metastatic phenotype and induces the apoptosis of glioblastoma cells by targeting LIMK kinase activity and activating the cofilin/G‑actin signaling cascade.International journal of molecular medicine · 2021Article
76 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin and small heat shock proteins (sHsps) are ubiquitous and multifaceted proteins that exist in 2 reversible forms, monomers and multimers, ie, the microfilament of the cytoskeleton and oligomers of the sHsps, generally, supposed to be in a spherical and hollow form. Two situations are described in the literature, where the properties of actin are modulated by sHsps; the actin polymerization is inhibited in vitro by some sHsps acting as capping proteins, and the actin cytoskeleton is protected by some sHsps against the disruption induced by various stressful conditions. We propose that a direct actin-sHsp interaction occurs to inhibit actin polymerization and to participate in the in vivo regulation of actin filament dynamics. Protection of the actin cytoskeleton would result from an F-actin-sHsp interaction in which microfilaments would be coated by small oligomers of phosphorylated sHsps. Both proteins share common structural motives suggesting direct binding sites, but they remain to be demonstrated. Some sHsps would behave with the actin cytoskeleton as actin-binding proteins capable of either capping a microfilament when present as a nonphosphorylated monomer or stabilizing and protecting the microfilament when organized in small, phosphorylated oligomers.
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