ArticleInternational journal of molecular sciences2022
The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- HSP27 regulates force-coordinated DDR1 condensate disassembly and liquid-to-gel phase transition.Science advances · 2026Article
- Review
- Overexpression of the human heat shock protein B1 alters obesity-related metabolic changes in a sex-dependent manner in a mouse model of metabolic syndrome.Biology of sex differences · 2025Article
- Article
- The role of membrane physiology in sHSP Lo18-lipid interaction and lipochaperone activity.Scientific reports · 2024Article
- X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model.Scientific reports · 2023Article
- Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis.Molecular plant pathology · 2023Article
- Review
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Membrane Proteins: Structure, Function and Motion.International journal of molecular sciences · 2022Article
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Authors and funding
10 authors at 1 institution in 2 countries.
Funding
Abstract
Small heat shock proteins (sHSPs) have been demonstrated to interact with lipids and modulate the physical state of membranes across species. Through these interactions, sHSPs contribute to the maintenance of membrane integrity. HSPB1 is a major sHSP in mammals, but its lipid interaction profile has so far been unexplored. In this study, we characterized the interaction between HSPB1 and phospholipids. HSPB1 not only associated with membranes via membrane-forming lipids, but also showed a strong affinity towards highly fluid membranes. It participated in the modulation of the physical properties of the interacting membranes by altering rotational and lateral lipid mobility. In addition, the in vivo expression of HSPB1 greatly affected the phase behavior of the plasma membrane under membrane fluidizing stress conditions. In light of our current findings, we propose a new function for HSPB1 as a membrane chaperone.
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Registered trials
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