ArticleThe Biochemical journal2007
Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 87 citations in OpenAlex.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Enhancement of Triple-Negative Breast Cancer-Specific Induction of Cell Death by Silver Nanoparticles by Combined Treatment with Proteotoxic Stress Response Inhibitors.Nanomaterials (Basel, Switzerland) · 2024Article
- BAG3: Nature's Quintessential Multi-Functional Protein Functions as a Ubiquitous Intra-Cellular Glue.Cells · 2023Review
- The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.International journal of molecular sciences · 2022Review
- The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.Scientific reports · 2021Article
- Delineation of temperature-humidity index (THI) as indicator of heat stress in riverine buffaloes (Bubalus bubalis) of a sub-tropical Indian region.Cell stress & chaperones · 2021Article
- Specific Roles of HSP27 S15 Phosphorylation Augmenting the Nuclear Function of HER2 to Promote Trastuzumab Resistance.Cancers · 2020Article
- Thermal Bioprinting Causes Ample Alterations of Expression of LUCAT1, IL6, CCL26, and NRN1L Genes and Massive Phosphorylation of Critical Oncogenic Drug Resistance Pathways in Breast Cancer Cells.Frontiers in bioengineering and biotechnology · 2020Article
- Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes.Cell stress & chaperones · 2019Review
- The N terminus of the small heat shock protein HSPB7 drives its polyQ aggregation-suppressing activity.The Journal of biological chemistry · 2019Article
- Nuclear export of ubiquitinated proteins via the UBIN-POST system.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- HSPB1 mutations causing hereditary neuropathy in humans disrupt non-cell autonomous protection of motor neurons.Experimental neurology · 2017Article
- Using bicistronic constructs to evaluate the chaperone activities of heat shock proteins in cells.Scientific reports · 2017Article
- Article
- Specific protein homeostatic functions of small heat-shock proteins increase lifespan.Aging cell · 2016Article
- Mechanisms of oxidative stress resistance in the brain: Lessons learned from hypoxia tolerant extremophilic vertebrates.Archives of biochemistry and biophysics · 2015Review
- Cross-omics comparison of stress responses in mesothelial cells exposed to heat- versus filter-sterilized peritoneal dialysis fluids.BioMed research international · 2015Article
- Drosophila melanogaster Hsp22: a mitochondrial small heat shock protein influencing the aging process.Frontiers in genetics · 2015Review
- Understanding the role of heat shock protein isoforms in male fertility, aging and apoptosis.The world journal of men's health · 2014Review
- TRNA mutations that affect decoding fidelity deregulate development and the proteostasis network in zebrafish.RNA biology · 2014Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In vitro, small Hsps (heat-shock proteins) have been shown to have chaperone function capable of keeping unfolded proteins in a form competent for Hsp70-dependent refolding. However, this has never been confirmed in living mammalian cells. In the present study, we show that Hsp27 (HspB1) translocates into the nucleus upon heat shock, where it forms granules that co-localize with IGCs (interchromatin granule clusters). Although heat-induced changes in the oligomerization status of Hsp27 correlate with its phosphorylation and nuclear translocation, Hsp27 phosphorylation alone is not sufficient for effective nuclear translocation of HspB1. Using firefly luciferase as a heat-sensitive reporter protein, we demonstrate that HspB1 expression in HspB1-deficient fibroblasts enhances protein refolding after heat shock. The positive effect of HspB1 on refolding is completely diminished by overexpression of Bag-1 (Bcl-2-associated athanogene), the negative regulator of Hsp70, consistent with the idea of HspB1 being the substrate holder for Hsp70. Although HspB1 and luciferase both accumulate in nuclear granules after heat shock, our results suggest that this is not related to the refolding activity of HspB1. Rather, granular accumulation may reflect a situation of failed refolding where the substrate is stored for subsequent degradation. Consistently, we found 20S proteasomes concentrated in nuclear granules of HspB1 after heat shock. We conclude that HspB1 contributes to an increased chaperone capacity of cells by binding unfolded proteins that are hereby kept competent for refolding by Hsp70 or that are sorted to nuclear granules if such refolding fails.
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