ArticleInternational journal of molecular sciences2020
STIP1/HOP Regulates the Actin Cytoskeleton through Interactions with Actin and Changes in Actin-Binding Proteins Cofilin and Profilin.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Profillin-1 and Transgelin-2: Actin Binding Proteins Expression in Early and Advanced Stages of Triple-Negative Breast Cancer Receiving Neoadjuvant Chemotherapy.Cancer reports (Hoboken, N.J.) · 2026Article
- STIP1/HOP promotes the formation of cytotoxic α-synuclein oligomers.Molecular neurodegeneration advances · 2026Article
- Sevoflurane Inhibits the Proliferation of Neural Precursor Cells and Neural Migration of Mice by Inducing Iron Metabolism Disorders.CNS neuroscience & therapeutics · 2025Article
- Functional Characterization ofInternational journal of molecular sciences · 2025Article
- Hsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication.The Journal of general virology · 2024Article
- Review
- DNA-PKcs Phosphorylates Cofilin2 to Induce Endothelial Dysfunction and Microcirculatory Disorder in Endotoxemic Cardiomyopathy.Research (Washington, D.C.) · 2024Article
- A pilot study of the relative number of circulating tumor cells and leukocytes containing actin-binding proteins in head and neck cancer patients.Journal of biomedical research · 2022Article
- Native Mass Spectrometry-Guided Screening Identifies Hit Fragments for HOP-HSP90 PPI Inhibition.Chembiochem : a European journal of chemical biology · 2022Article
- Morphological and Molecular Responses ofInternational journal of molecular sciences · 2022Article
- Prion Protein at the Leading Edge: Its Role in Cell Motility.International journal of molecular sciences · 2020Review
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Authors and funding
12 authors at 1 institution in 2 countries.
Funding
Abstract
Cell migration plays a vital role in both health and disease. It is driven by reorganization of the actin cytoskeleton, which is regulated by actin-binding proteins cofilin and profilin. Stress-inducible phosphoprotein 1 (STIP1) is a well-described co-chaperone of the Hsp90 chaperone system, and our findings identify a potential regulatory role of STIP1 in actin dynamics. We show that STIP1 can be isolated in complex with actin and Hsp90 from HEK293T cells and directly interacts with actin in vitro via the C-terminal TPR2AB-DP2 domain of STIP1, potentially due to a region spanning two putative actin-binding motifs. We found that STIP1 could stimulate the in vitro ATPase activity of actin, suggesting a potential role in the modulation of F-actin formation. Interestingly, while STIP1 depletion in HEK293T cells had no major effect on total actin levels, it led to increased nuclear accumulation of actin, disorganization of F-actin structures, and an increase and decrease in cofilin and profilin levels, respectively. This study suggests that STIP1 regulates the cytoskeleton by interacting with actin, or via regulating the ratio of proteins known to affect actin dynamics.
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Registered trials
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