ArticleMolecular biology of the cell2022
Phosphorylation of the small heat shock protein HspB1 regulates cytoskeletal recruitment and cell motility.
Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
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- Neuropathy-Associated HSPB1 Mutant Impairs Neuronal Mechanoadaptation and Axonal Regeneration.Cells · 2026Article
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- Genome-wide identification of the cotton ANK gene family and functional study of GhANK169 in response to heat stress.BMC plant biology · 2025Article
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- Integrated transcriptomic and proteomic analyses identify the TLR2-CXCR4 axis as a regulator of endothelial cell migration under simulated microgravity.Frontiers in physiology · 2025Article
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- The biphasic role of Hspb1 on ferroptotic cell death in Parkinson's disease.Theranostics · 2024Article
- HSPB1 alleviates acute-on-chronic liver failure via the P53/Bax pathway.Open life sciences · 2024Article
- Musashi-2 Deficiency Triggers Colorectal Cancer Ferroptosis by Downregulating the MAPK Signaling Cascade to Inhibit HSPB1 Phosphorylation.Biological procedures online · 2023Article
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- Mechanistic insights into heat shock protein 27, a potential therapeutic target for cardiovascular diseases.Frontiers in cardiovascular medicine · 2023Review
- From mesenchymal niches to engineeredMaterials today. Bio · 2022Article
- Timescale-dependent Phosphoproteomic Remodeling and Motility-associated Adaptation under Chronic Cabozantinib Exposure in Renal Cell Carcinoma.Cancer genomics & proteomicsArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The small heat shock protein HspB1, also known as Hsp25/27, is a ubiquitously expressed molecular chaperone that responds to mechanical cues. Uniaxial cyclic stretch activates the p38 mitogen-activated protein kinase (MAPK) signaling cascade and increases the phosphorylation of HspB1. Similar to the mechanosensitive cytoskeletal regulator zyxin, phospho-HspB1 is recruited to features of the stretch-stimulated actin cytoskeleton. To evaluate the role of HspB1 and its phosphoregulation in modulating cell function, we utilized CRISPR/Cas9-edited HspB1-null cells and determined they were altered in behaviors such as actin cytoskeletal remodeling, cell spreading, and cell motility. In our model system, expression of WT HspB1, but not nonphosphorylatable HspB1, rescued certain characteristics of the HspB1-null cells including the enhanced cell motility of HspB1-null cells and the deficient actin reinforcement of stretch-stimulated HspB1-null cells. The recruitment of HspB1 to high-tension structures in geometrically constrained cells, such as actin comet tails emanating from focal adhesions, also required a phosphorylatable HspB1. We show that mechanical signals activate posttranslational regulation of the molecular chaperone, HspB1, and are required for normal cell behaviors including actin cytoskeletal remodeling, cell spreading, and cell migration.
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