ArticleMarine drugs2015
The effect of cholesterol on the long-range network of interactions established among sea anemone Sticholysin II residues at the water-membrane interface.
Article in Marine drugs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.Science advances · 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
- Cytotoxic effect of sea anemone pore-forming toxin on K562 chronic myeloid leukemia cells.Veterinary research forum : an international quarterly journal · 2021Article
- Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea AnemoneInternational journal of molecular sciences · 2020Review
- Pore-Forming Proteins from Cnidarians and Arachnids as Potential Biotechnological Tools.Toxins · 2019Article
- Sticholysin, Sphingomyelin, and Cholesterol: A Closer Look at a Tripartite Interaction.Biophysical journal · 2019Article
- Multigene Family of Pore-Forming Toxins from Sea AnemoneMarine drugs · 2018Article
- Identification of unusual peptides with new Cys frameworks in the venom of the cold-water sea anemone Cnidopus japonicus.Scientific reports · 2017Article
- Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.Biophysical reviews · 2017Review
- Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores.The Journal of biological chemistry · 2016Article
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 α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members. These proteins remain stably folded in water, but upon interaction with lipid bilayers, they oligomerize to form a pore. This event is triggered by the presence of sphingomyelin (SM), but cholesterol (Chol) facilitates pore formation. Membrane attachment and pore formation require changes involving long-distance rearrangements of residues located at the protein-membrane interface. The influence of Chol on membrane recognition, oligomerization, and/or pore formation is now studied using StnII variants, which are characterized in terms of their ability to interact with model membranes in the presence or absence of Chol. The results obtained frame Chol not only as an important partner for SM for functional membrane recognition but also as a molecule which significantly reduces the structural requirements for the mentioned conformational rearrangements to occur. However, given that the DOPC:SM:Chol vesicles employed display phase coexistence and have domain boundaries, the observed effects could be also due to the presence of these different phases on the membrane. In addition, it is also shown that the Arg51 guanidinium group is strictly required for membrane recognition, independently of the presence of Chol.
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