ArticlePloS one2013
Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1).
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Ascorbic acid mitigates the impact of oxidative stress in a human model of febrile seizure and mesial temporal lobe epilepsy.Scientific reports · 2024Article
- Polo-Like Kinase 2 Plays an Essential Role in Cytoprotection against MG132-Induced Proteasome Inhibition via Phosphorylation of Serine 19 in HSPB5.International journal of molecular sciences · 2022Article
- Small heat-shock proteins and their role in mechanical stress.Cell stress & chaperones · 2020Review
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- Regulation of small heat-shock proteins by hetero-oligomer formation.The Journal of biological chemistry · 2020Article
- Progression of the role of CRYAB in signaling pathways and cancers.OncoTargets and therapy · 2019Review
- Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.Cell stress & chaperones · 2017Review
- Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer.Cancer biomarkers : section A of Disease markers · 2016Article
- NFκB is a central regulator of protein quality control in response to protein aggregation stresses via autophagy modulation.Molecular biology of the cell · 2016Article
- Differential role of arginine mutations on the structure and functions of α-crystallin.Biochimica et biophysica acta · 2016Review
- Small heat-shock proteins: important players in regulating cellular proteostasis.Cellular and molecular life sciences : CMLS · 2015Review
- Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners.PloS one · 2015Article
- HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Cancers · 2014Article
- Peptide aptamers: tools to negatively or positively modulate HSPB1(27) function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Neuropathy- and myopathy-associated mutations in human small heat shock proteins: Characteristics and evolutionary history of the mutation sites.Mutation research. Reviews in mutation researchReview
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several human small heat shock proteins (sHsps) are phosphorylated oligomeric chaperones that enhance stress resistance. They are characterized by their ability to interact and form polydispersed hetero-oligomeric complexes. We have analyzed the cellular consequences of the stable expression of either wild type HspB5 or its cataracts and myopathies inducing R120G mutant in growing and oxidative stress treated HeLa cells that originally express only HspB1. Here, we describe that wild type and mutant HspB5 induce drastic and opposite effects on cell morphology and oxidative stress resistance. The cellular distribution and phosphorylation of these polypeptides as well as the oligomerization profile of the resulting hetero-oligomeric complexes formed by HspB1 with the two types of exogenous polypeptides revealed the dominant effects induced by HspB5 polypeptides towards HspB1. The R120G mutation enhanced the native size and salt resistance of HspB1-HspB5 complex. However, in oxidative conditions the interaction between HspB1 and mutant HspB5 was drastically modified resulting in the aggregation of both partners. The mutation also induced the redistribution of HspB1 phosphorylated at serine 15, originally observed at the level of the small oligomers that do not interact with wild type HspB5, to the large oligomeric complex formed with mutant HspB5. This phosphorylation stabilized the interaction of HspB1 with mutant HspB5. A dominant negative effect towards HspB1 appears therefore as an important event in the cellular sensitivity to oxidative stress mediated by mutated HspB5 expression. These observations provide novel data that describe how a mutated sHsp can alter the protective activity of another member of this family of chaperones.
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