The metamorphic transformation of a water-soluble monomeric protein into an oligomeric transmembrane pore

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dc.book.titleAdvances in Biomembranes and Lipid Self-Assembly
dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorRivera de la Torre, Esperanza
dc.contributor.authorPalacios Ortega, Juan
dc.contributor.authorGavilanes, José G.
dc.contributor.authorMartínez del Pozo, Álvaro
dc.date.accessioned2023-06-18T00:23:25Z
dc.date.available2023-06-18T00:23:25Z
dc.date.issued2017
dc.description.abstractSea anemones produce venoms containing different toxic molecules. Among them, actinoporins are some of the best characterized ones. They constitute a family of toxic polypeptides that belong to the much larger group of pore-forming toxins. Actinoporins remain mostly monomeric and stably folded in aqueous solution but, upon interaction with lipid membranes of specific composition, they become oligomeric integral membrane structures to build a pore. They insert an α-helix stretch within biological membranes, forming cation-selective pores with a diameter of 1–2 nm, which result in a colloid osmotic shock that leads to cell death. They are believed to participate in functions like predation, defense, and digestion and have been shown to be lethal for small crustaceans, mollusks, and fish. The best-known actinoporins are equinatoxin II (from Actinia equina), fragaceatoxin C (from Actinia fragacea), and sticholysins I and II (from Stichodactyla helianthus). In order to fully understand the pore formation mechanism of these proteins, several approaches have been used: (i) characterization of natural and artificial variants of actinoporins to determine the role of specific residues, (ii) study of their water-soluble and transmembrane structures, and (iii) employment of different lipids to evaluate the influence of membrane properties and composition. Further research is still needed, however, in order to fully understand the complex mechanism underlying actinoporins’ functionality.
dc.description.departmentSección Deptal. de Bioquímica y Biología Molecular (Biológicas)
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Ciencias Biológicas
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/46674
dc.identifier.doi10.1016/bs.abl.2017.06.004
dc.identifier.isbn9780128120798
dc.identifier.officialurlhttps://www.sciencedirect.com/science/article/pii/S2451963417300201
dc.identifier.urihttps://hdl.handle.net/20.500.14352/19495
dc.issue.number26
dc.language.isoeng
dc.page.final47
dc.page.initial1
dc.page.total199
dc.publication.placeAmsterdam
dc.publisherEslsevier
dc.relation.ispartofseriesAdvances in Biomembranes and Lipid Self-Assembly
dc.rights.accessRightsrestricted access
dc.subject.cdu577.112
dc.subject.keywordSea anemones
dc.subject.keywordPore-forming toxins
dc.subject.keywordSphingomyelin
dc.subject.keywordCholesterol
dc.subject.keywordEquinatoxin
dc.subject.keywordFragaceatoxin
dc.subject.keywordSticholysin
dc.subject.ucmBioquímica (Biología)
dc.subject.unesco2302 Bioquímica
dc.titleThe metamorphic transformation of a water-soluble monomeric protein into an oligomeric transmembrane pore
dc.typebook part
dc.volume.number2
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
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