ArticleProceedings of the National Academy of Sciences of the United States of America1986
Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024Review
- Identification of FAM53C as a cytosolic-anchoring inhibitory binding protein of the kinase DYRK1A.Life science alliance · 2023Article
- Expression of hypoxia-inducible genes is suppressed in altered gravity due to impaired nuclear HIF1α accumulation.Scientific reports · 2023Article
- Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance.Cells · 2022Review
- Hsp90: From Cellular to Organismal Proteostasis.Cells · 2022Review
- Unravelling the neuroprotective mechanisms of carotenes in differentiated human neural cells: Biochemical and proteomic approaches.Food chemistry. Molecular sciences · 2022Article
- Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021Review
- Nonredundant functions of Mycobacterium tuberculosis chaperones promote survival under stress.Molecular microbiology · 2021Article
- Validation of reference genes for the normalization of RT-qPCR gene expression in Acanthamoeba spp.Scientific reports · 2020Article
- STIP1/HOP Regulates the Actin Cytoskeleton through Interactions with Actin and Changes in Actin-Binding Proteins Cofilin and Profilin.International journal of molecular sciences · 2020Article
- Non-enzymatic cleavage of Hsp90 by oxidative stress leads to actin aggregate formation: A novel gain-of-function mechanism.Redox biology · 2019Article
- The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease.International journal of molecular sciences · 2018Review
- Dysregulated fibronectin trafficking by Hsp90 inhibition restricts prostate cancer cell invasion.Scientific reports · 2018Article
- Bipartite Role of Heat Shock Protein 90 (Hsp90) Keeps CRAF Kinase Poised for Activation.The Journal of biological chemistry · 2016Article
- HSP90AB1: Helping the good and the bad.Gene · 2016Review
- Multifunctional Microtubule-Associated Proteins in Plants.Frontiers in plant science · 2016Review
- WISp39 binds phosphorylated Coronin 1B to regulate Arp2/3 localization and Cofilin-dependent motility.The Journal of cell biology · 2015Article
- The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation.The Journal of biological chemistry · 2014Article
- Regulation of endothelial nitric oxide synthase activity by protein-protein interaction.Current pharmaceutical design · 2014Review
- HDAC8 substrates: Histones and beyond.Biopolymers · 2013Review
9 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two high molecular weight heat shock proteins, HSP90 (Mr, 90,000) and HSP100 (Mr, 100,000), were separately purified from extracts of cultured cells of a mouse lymphoma cell line, L5178Y. Both of the HSPs exist in homodimeric form under physiological conditions. Their physicochemical properties are quite similar to each other. Each of the purified HSPs was shown to coprecipitate with rabbit skeletal muscle actin under actin-polymerizing conditions. Both HSP90 and HSP100 increased the low-shear viscosity of filamentous actin solutions in a dose-dependent manner, which suggests that these HSPs cross-link actin filaments. Although some molecular properties and the effects described above on actin solution of HSP90 and HSP100 resemble those of alpha-actinin, the HSPs were distinguished from alpha-actinin by various means, including visualization of molecular shapes by electron microscopy with the aid of the low-angle rotary shadowing technique. Immunofluorescence staining by specific antisera against HSP90 revealed that HSP90 was localized in ruffling membranes in addition to the cytoplasmic space.
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