ArticleBiophysical journal2019
Sticholysin, Sphingomyelin, and Cholesterol: A Closer Look at a Tripartite Interaction.
Article in Biophysical journal, 2019. 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, 19 citations in OpenAlex.
- Senotoxins target senescence via lipid binding specificity, ion imbalance and lipidome remodeling.Nature aging · 2026Article
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Recombinant HALT-1 induces mitochondrial-associated apoptotic mechanism in HeLa cells.Scientific reports · 2025Article
- Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.Science advances · 2025Article
- Cryo-EM structures of a protein pore reveal a cluster of cholesterol molecules and diverse roles of membrane lipids.Nature communications · 2025Article
- Determination of the boundary lipids of sticholysins using tryptophan quenching.Scientific reports · 2022Article
- Sea Anemones, Actinoporins, and Cholesterol.International journal of molecular sciences · 2022Review
- Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea AnemoneInternational journal of molecular sciences · 2020Review
- Actinoporins: From the Structure and Function to the Generation of Biotechnological and Therapeutic Tools.Biomolecules · 2020Review
- Pore-Forming Proteins from Cnidarians and Arachnids as Potential Biotechnological Tools.Toxins · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actinoporins are a group of soluble toxic proteins that bind to membranes containing sphingomyelin (SM) and oligomerize to form pores. Sticholysin II (StnII) is a member of the actinoporin family produced by Stichodactyla helianthus. Cholesterol (Chol) is known to enhance the activity of StnII. However, the molecular mechanisms behind this activation have remained obscure, although the activation is not Chol specific but rather sterol specific. To further explore how bilayer lipids affect or are affected by StnII, we have used a multiprobe approach (fluorescent analogs of both Chol and SM) in combination with a series of StnII tryptophan (Trp) mutants to study StnII/bilayer interactions. First, we compared StnII bilayer permeabilization in the presence of Chol or oleoyl-ceramide (OCer). The comparison was done because both Chol and OCer have a 1-hydroxyl, which helps to orient the molecule in the bilayer (although OCer has additional polar functional groups). Both Chol and OCer also have increased affinity for SM, which StnII may recognize. However, our results show that only Chol was able to activate StnII-induced bilayer permeabilization; OCer failed to activate it. To further examine possible Chol/StnII interactions, we measured Förster resonance energy transfer between Trp in StnII and cholestatrienol, a fluorescent analog of Chol. We could show higher Förster resonance energy transfer efficiency between cholestatrienol and Trps in position 100 and 114 of StnII when compared to three other Trp positions further away from the bilayer binding region of StnII. Taken together, our results suggest that StnII was able to attract Chol to its vicinity, maybe by showing affinity for Chol. SM interactions are known to be important for StnII binding to bilayers, and Chol is known to facilitate subsequent permeabilization of the bilayers by StnII. Our results help to better understand the role of these important membrane lipids for the bilayer properties of StnII.
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