Pore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging

DC FieldValueLanguage
dc.contributor.authorMargheritis, Eleonora
dc.contributor.authorKappelhoff, Shirin
dc.contributor.authorCosentino, Katia
dc.date.accessioned2023-07-12T06:53:46Z-
dc.date.available2023-07-12T06:53:46Z-
dc.date.issued2023
dc.identifier.urihttp://osnascholar.ub.uni-osnabrueck.de/handle/unios/71820-
dc.description.abstractPore-forming proteins (PFPs) play a central role in many biological processes related to infection, immunity, cancer, and neurodegeneration. A common feature of PFPs is their ability to form pores that disrupt the membrane permeability barrier and ion homeostasis and generally induce cell death. Some PFPs are part of the genetically encoded machinery of eukaryotic cells that are activated against infection by pathogens or in physiological programs to carry out regulated cell death. PFPs organize into supramolecular transmembrane complexes that perforate membranes through a multistep process involving membrane insertion, protein oligomerization, and finally pore formation. However, the exact mechanism of pore formation varies from PFP to PFP, resulting in different pore structures with different functionalities. Here, we review recent insights into the molecular mechanisms by which PFPs permeabilize membranes and recent methodological advances in their characterization in artificial and cellular membranes. In particular, we focus on single-molecule imaging techniques as powerful tools to unravel the molecular mechanistic details of pore assembly that are often obscured by ensemble measurements, and to determine pore structure and functionality. Uncovering the mechanistic elements of pore formation is critical for understanding the physiological role of PFPs and developing therapeutic approaches.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft [SFB944-P26, SFB1557-P5]; Research in the laboratory is funded by Deutsche Forschungsgemeinschaft (DFG) grant numbers SFB944-P26 and SFB1557-P5.
dc.language.isoen
dc.publisherMDPI
dc.relation.ispartofINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
dc.subjectBiochemistry & Molecular Biology
dc.subjectChemistry
dc.subjectChemistry, Multidisciplinary
dc.subjectCOLICIN IA CHANNEL
dc.subjectCRYSTAL-STRUCTURES
dc.subjectEQUINATOXIN-II
dc.subjectGASDERMIN D
dc.subjectLIPID-BILAYERS
dc.subjectLISTERIA-MONOCYTOGENES
dc.subjectMASS PHOTOMETRY
dc.subjectPOLYMER-SUPPORTED MEMBRANES
dc.subjectpore functionality
dc.subjectpore-forming proteins
dc.subjectprotein complex stoichiometry
dc.subjectsingle-molecule fluorescence microscopy
dc.subjectsuper-resolution microscopy
dc.subjectSUPERRESOLUTION MICROSCOPY
dc.subjectTOXIN
dc.titlePore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging
dc.typereview
dc.identifier.doi10.3390/ijms24054528
dc.identifier.isiISI:000947325200001
dc.description.volume24
dc.description.issue5
dc.identifier.eissn1422-0067
dc.publisher.placeST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
dcterms.isPartOf.abbreviationInt. J. Mol. Sci.
dcterms.oaStatusGreen Published, gold
local.import.remainsaffiliations : University Osnabruck; University Osnabruck
local.import.remainsweb-of-science-index : Science Citation Index Expanded (SCI-EXPANDED)
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidCoKa893-
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