{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,12]],"date-time":"2025-12-12T15:56:21Z","timestamp":1765554981393,"version":"build-2065373602"},"reference-count":87,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2023,6,7]],"date-time":"2023-06-07T00:00:00Z","timestamp":1686096000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Fight for Sight","award":["1584\/85","SAC014","662287"],"award-info":[{"award-number":["1584\/85","SAC014","662287"]}]},{"DOI":"10.13039\/501100000305","name":"National Eye Research Charity","doi-asserted-by":"publisher","award":["1584\/85","SAC014","662287"],"award-info":[{"award-number":["1584\/85","SAC014","662287"]}],"id":[{"id":"10.13039\/501100000305","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Euratom research and training programme 2014\u20132018 in the framework of the CONCERT","award":["1584\/85","SAC014","662287"],"award-info":[{"award-number":["1584\/85","SAC014","662287"]}]},{"name":"Biophysical Sciences Institute","award":["1584\/85","SAC014","662287"],"award-info":[{"award-number":["1584\/85","SAC014","662287"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Background: BFSP1 (beaded filament structural protein 1) is a plasma membrane, Aquaporin 0 (AQP0\/MIP)-associated intermediate filament protein expressed in the eye lens. BFSP1 is myristoylated, a post-translation modification that requires caspase cleavage at D433. Bioinformatic analyses suggested that the sequences 434\u2013452 were \u03b1-helical and amphipathic. Methods and Results: By CD spectroscopy, we show that the addition of trifluoroethanol induced a switch from an intrinsically disordered to a more \u03b1-helical conformation for the residues 434\u2013467. Recombinantly produced BFSP1 fragments containing this amphipathic helix bind to lens lipid bilayers as determined by surface plasmon resonance (SPR). Lastly, we demonstrate by transient transfection of non-lens MCF7 cells that these same BFSP1 C-terminal sequences localise to plasma membranes and to cytoplasmic vesicles. These can be co-labelled with the vital dye, lysotracker, but other cell compartments, such as the nuclear and mitochondrial membranes, were negative. The N-terminal myristoylation of the amphipathic helix appeared not to change either the lipid affinity or membrane localisation of the BFSP1 polypeptides or fragments we assessed by SPR and transient transfection, but it did appear to enhance its helical content. Conclusions: These data support the conclusion that C-terminal sequences of human BFSP1 distal to the caspase site at G433 have independent membrane binding properties via an adjacent amphipathic helix.<\/jats:p>","DOI":"10.3390\/cells12121580","type":"journal-article","created":{"date-parts":[[2023,6,8]],"date-time":"2023-06-08T01:34:32Z","timestamp":1686188072000},"page":"1580","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Independent Membrane Binding Properties of the Caspase Generated Fragments of the Beaded Filament Structural Protein 1 (BFSP1) Involves an Amphipathic Helix"],"prefix":"10.3390","volume":"12","author":[{"given":"Miguel","family":"Jarrin","sequence":"first","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexia A.","family":"Kalligeraki","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alice","family":"Uwineza","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chris S.","family":"Cawood","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adrian P.","family":"Brown","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9078-9716","authenticated-orcid":false,"given":"Edward N.","family":"Ward","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Khoa","family":"Le","sequence":"additional","affiliation":[{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"},{"name":"Department of Biological Structure, University of Washington, Seattle, WA 98195, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1423-8103","authenticated-orcid":false,"given":"Stefanie","family":"Freitag-Pohl","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Durham University, Lower Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ehmke","family":"Pohl","sequence":"additional","affiliation":[{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"},{"name":"Department of Chemistry, Durham University, Lower Mountjoy, South Road, Durham DH1 3LE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bence","family":"Kiss","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Medical Chemistry, Medical School, University of P\u00e9cs, 7624 P\u00e9cs, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Antal","family":"Tapodi","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"},{"name":"Department of Biochemistry and Medical Chemistry, Medical School, University of P\u00e9cs, 7624 P\u00e9cs, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0644-4123","authenticated-orcid":false,"given":"Roy A.","family":"Quinlan","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Upper Mountjoy Science Site, The University of Durham, South Road, Durham DH1 3LE, UK"},{"name":"Biophysical Sciences Institute, Durham University, Upper Mountjoy, South Road, Durham DH1 3LE, UK"},{"name":"Department of Biological Structure, University of Washington, Seattle, WA 98195, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,6,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"102537","DOI":"10.1016\/j.jbc.2022.102537","article-title":"Insights into the Biochemical and Biophysical Mechanisms Mediating The Longevity of the Transparent Optics of the Eye Lens","volume":"298","author":"Quinlan","year":"2022","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.yexcr.2004.11.021","article-title":"Seeing is believing! The optical properties of the eye lens are dependent upon a functional intermediate filament cytoskeleton","volume":"305","author":"Perng","year":"2005","journal-title":"Exp. Cell. Res."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0014-4835(95)80009-3","article-title":"In vitro studies on the assembly properties of the lens beaded filament proteins: Co-assembly with a-crystallin but not with vimentin","volume":"60","author":"Carter","year":"1995","journal-title":"Exp. Eye Res."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0014-4835(72)90136-4","article-title":"Electron microscope observations on some structural proteins of the chick lens","volume":"14","author":"Maisel","year":"1972","journal-title":"Exp. Eye Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1172\/JCI38277","article-title":"Functions of the intermediate filament cytoskeleton in the eye lens","volume":"119","author":"Song","year":"2009","journal-title":"J. Clin. Investig."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"108662","DOI":"10.1016\/j.exer.2021.108662","article-title":"Inherited cataracts: Genetic mechanisms and pathways new and old","volume":"209","author":"Shiels","year":"2021","journal-title":"Exp. Eye Res."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"3860","DOI":"10.1167\/iovs.10-6231","article-title":"Intermediate filaments regulate tissue size and stiffness in the murine lens","volume":"52","author":"Fudge","year":"2011","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/S0014-4835(02)00330-5","article-title":"Knockout of the intermediate filament protein CP49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract","volume":"76","author":"Sandilands","year":"2003","journal-title":"Exp. Eye Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.exer.2003.09.001","article-title":"Bfsp2 mutation found in mouse 129 strains causes the loss of CP49 and induces vimentin-dependent changes in the lens fibre cell cytoskeleton","volume":"78","author":"Sandilands","year":"2004","journal-title":"Exp. Eye Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"5252","DOI":"10.1167\/iovs.03-0224","article-title":"Targeted deletion of the lens fiber cell-specific intermediate filament protein filensin","volume":"44","author":"Alizadeh","year":"2003","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_11","first-page":"3722","article-title":"Targeted genomic deletion of the lens-specific intermediate filament protein CP49","volume":"43","author":"Alizadeh","year":"2002","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1166\/jnn.2007.510","article-title":"Motility and structural polymorphism of polymer-actin complex gel","volume":"7","author":"Kwon","year":"2007","journal-title":"J. Nanosci. Nanotechnol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.exer.2008.11.007","article-title":"Lens intermediate filaments","volume":"88","author":"FitzGerald","year":"2009","journal-title":"Exp. Eye Res."},{"key":"ref_14","unstructured":"Landsbury, A., Perng, M.D., Pohl, E., and Quinlan, R.A. (2010). Small Stress Proteins and Human Diseases, Nova Science Publishers Inc."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"16898","DOI":"10.1038\/s41598-020-73625-9","article-title":"Three-dimensional data capture and analysis of intact eye lenses evidences emmetropia-associated changes in epithelial cell organization","volume":"10","author":"Kalligeraki","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"471","DOI":"10.3109\/02713689109001754","article-title":"Immunologic conservation of the fiber cell beaded filament","volume":"10","author":"FitzGerald","year":"1991","journal-title":"Curr. Eye Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"2180","DOI":"10.1016\/j.yexcr.2007.04.005","article-title":"Insights into the beaded filament of the eye lens","volume":"313","author":"Zhang","year":"2007","journal-title":"Exp. Cell. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"107585","DOI":"10.1016\/j.exer.2019.02.001","article-title":"BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability","volume":"185","author":"Tapodi","year":"2019","journal-title":"Exp. Eye Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0378-1119(97)00419-8","article-title":"Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: Implications for protein classification and assembly","volume":"201","author":"Masaki","year":"1997","journal-title":"Gene"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1167\/iovs.09-4565","article-title":"Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49","volume":"51","author":"Wang","year":"2010","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.biochi.2010.10.018","article-title":"Post-translational myristoylation: Fat matters in cellular life and death","volume":"93","author":"Martin","year":"2011","journal-title":"Biochimie"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1086112","DOI":"10.3389\/fphys.2023.1086112","article-title":"Full-length huntingtin is palmitoylated at multiple sites and post-translationally myristoylated following caspase-cleavage","volume":"14","author":"Sanders","year":"2023","journal-title":"Front. Physiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"167605","DOI":"10.1016\/j.jmb.2022.167605","article-title":"SVMyr: A Web Server Detecting Co- and Post-translational Myristoylation in Proteins","volume":"434","author":"Madeo","year":"2022","journal-title":"J. Mol. Biol."},{"key":"ref_24","first-page":"238","article-title":"Filensin is proteolytically processed during lens fiber cell differentiation by multiple independant pathways","volume":"67","author":"Sandilands","year":"1995","journal-title":"Eur. J. Cell. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"108134","DOI":"10.1016\/j.exer.2020.108134","article-title":"Localization of the lens intermediate filament switch by imaging mass spectrometry","volume":"198","author":"Wang","year":"2020","journal-title":"Exp. Eye Res."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1242\/jcs.108.4.1397","article-title":"Vimentin and CP49\/Filensin form distinct networks in the lens which are independantly modulated during lens fibre cell differentiation","volume":"108","author":"Sandilands","year":"1995","journal-title":"J. Cell. Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"102014","DOI":"10.1016\/j.redox.2021.102014","article-title":"Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress","volume":"44","author":"Griesser","year":"2021","journal-title":"Redox Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"5304","DOI":"10.1111\/febs.15321","article-title":"Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro","volume":"287","author":"Szczepanowski","year":"2020","journal-title":"Febs J."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1002\/cm.21679","article-title":"Posttranslational modifications of the cytoskeleton","volume":"78","author":"MacTaggart","year":"2021","journal-title":"Cytoskeleton"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e35336","DOI":"10.7554\/eLife.35336","article-title":"The sweet side of vimentin","volume":"7","author":"Snider","year":"2018","journal-title":"Elife"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.exer.2017.02.012","article-title":"Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin","volume":"159","author":"Wang","year":"2017","journal-title":"Exp. Eye Res."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Schey, K.L., Petrova, R.S., Gletten, R.B., and Donaldson, P.J. (2017). The Role of Aquaporins in Ocular Lens Homeostasis. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18122693"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"108645","DOI":"10.1016\/j.exer.2021.108645","article-title":"Deletion of beaded filament proteins or the C-terminal end of Aquaporin 0 causes analogous abnormal distortion aberrations in mouse lens","volume":"209","author":"Varadaraj","year":"2021","journal-title":"Exp. Eye Res."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1242\/jcs.103.3.709","article-title":"Membrane-binding properties of filensin, a cytoskeletal protein of the lens fibre cells","volume":"103","author":"Brunkener","year":"1992","journal-title":"J. Cell. Sci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"8349","DOI":"10.1167\/iovs.15-18273","article-title":"Proteomic Analysis of Lipid Raft-Like Detergent-Resistant Membranes of Lens Fiber Cells","volume":"56","author":"Wang","year":"2015","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2967","DOI":"10.1002\/j.1460-2075.1988.tb03159.x","article-title":"Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations","volume":"7","author":"Milks","year":"1988","journal-title":"EMBO J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"101139","DOI":"10.1016\/j.plipres.2021.101139","article-title":"Mapping the myristoylome through a complete understanding of protein myristoylation biochemistry","volume":"85","author":"Giglione","year":"2022","journal-title":"Progress. Lipid Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1007\/s12154-009-0032-8","article-title":"Protein myristoylation in health and disease","volume":"3","author":"Wright","year":"2010","journal-title":"J. Chem. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.bbamem.2004.12.003","article-title":"A structural study of the myristoylated N-terminus of ARF1","volume":"1668","author":"Harroun","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.str.2008.10.020","article-title":"Structure and membrane interaction of myristoylated ARF1","volume":"17","author":"Liu","year":"2009","journal-title":"Structure"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"16643","DOI":"10.1074\/jbc.RA120.014999","article-title":"The amphipathic helices of Arfrp1 and Arl14 are sufficient to determine subcellular localizations","volume":"295","author":"Yang","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"8130","DOI":"10.1074\/jbc.M111289200","article-title":"An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A","volume":"277","author":"Brass","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1093\/bioinformatics\/btn392","article-title":"HELIQUEST: A web server to screen sequences with specific alpha-helical properties","volume":"24","author":"Gautier","year":"2008","journal-title":"Bioinformatics"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"5577","DOI":"10.3390\/ijms12095577","article-title":"New user-friendly approach to obtain an eisenberg plot and its use as a practical tool in protein sequence analysis","volume":"12","author":"Keller","year":"2011","journal-title":"Int. J. Mol. Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s00232-012-9498-3","article-title":"Prediction of lipid-binding regions in cytoplasmic and extracellular loops of membrane proteins as exemplified by protein translocation membrane proteins","volume":"246","author":"Keller","year":"2013","journal-title":"J. Membr. Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4438","DOI":"10.1038\/s41467-021-24773-7","article-title":"flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions","volume":"12","author":"Hu","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1109\/TCBB.2020.3029274","article-title":"Ab-Initio Membrane Protein Amphipathic Helix Structure Prediction Using Deep Neural Networks","volume":"19","author":"Feng","year":"2022","journal-title":"IEEE\/ACM Trans. Comput. Biol. Bioinform.\/IEEE ACM"},{"key":"ref_48","unstructured":"(2023). UniProt: The Universal Protein Knowledgebase in 2023. Nucleic Acids Res., 51, D523\u2013D531."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1093\/bioinformatics\/btm076","article-title":"COBALT: Constraint-based alignment tool for multiple protein sequences","volume":"23","author":"Papadopoulos","year":"2007","journal-title":"Bioinformatics"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"D439","DOI":"10.1093\/nar\/gkab1061","article-title":"AlphaFold Protein Structure Database: Massively expanding the structural coverage of protein-sequence space with high-accuracy models","volume":"50","author":"Varadi","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"831740","DOI":"10.3389\/fmolb.2022.831740","article-title":"iCn3D: From Web-Based 3D Viewer to Structural Analysis Tool in Batch Mode","volume":"9","author":"Wang","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1007\/s12192-017-0788-7","article-title":"\u03b1B-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments","volume":"22","author":"Sharma","year":"2017","journal-title":"Cell. Stress. Chaperones"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0091-679X(04)78021-8","article-title":"The intermediate filament systems in the eye lens","volume":"78","author":"Perng","year":"2004","journal-title":"Intermed. Filam. Cytoskelet."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"100057","DOI":"10.1016\/j.arres.2022.100057","article-title":"Identification and quantification of ionising radiation-induced oxysterol formation in membranes of lens fibre cells","volume":"7","author":"Uwineza","year":"2023","journal-title":"Adv. Redox Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1139\/y59-099","article-title":"A rapid method of total lipid extraction and purification","volume":"37","author":"Bligh","year":"1959","journal-title":"Can. J. Biochem. Physiol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1021\/bi0112457","article-title":"alpha-Crystallin Chaperone-like Activity and Membrane Binding in Age-Related Cataracts","volume":"41","author":"Cobb","year":"2002","journal-title":"Biochemistry"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1006\/exer.1996.0130","article-title":"Binding capacity of alpha-crystallin to bovine lens lipids","volume":"63","author":"Borchman","year":"1996","journal-title":"Exp. Eye Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"12179","DOI":"10.1073\/pnas.182199699","article-title":"Mechanism by which 2,2,2-trifluoroethanol\/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study","volume":"99","author":"Roccatano","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/S0167-4838(01)00271-0","article-title":"Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis","volume":"1550","author":"Konno","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1002\/pro.4153","article-title":"DichroWeb, a website for calculating protein secondary structure from circular dichroism spectroscopic data","volume":"31","author":"Miles","year":"2022","journal-title":"Protein Sci."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1006\/abio.2000.4880","article-title":"Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal. Biochem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1006\/abio.2000.4879","article-title":"Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal. Biochem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1896","DOI":"10.1038\/nprot.2007.261","article-title":"Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips","volume":"2","author":"Rappsilber","year":"2007","journal-title":"Nat. Protoc."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"277","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1248\/bpb.30.859","article-title":"Autophagy preceded apoptosis in oridonin-treated human breast cancer MCF-7 cells","volume":"30","author":"Cui","year":"2007","journal-title":"Biol. Pharm. Bull."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"W208","DOI":"10.1093\/nar\/gki433","article-title":"GraBCas: A bioinformatics tool for score-based prediction of Caspase- and Granzyme B-cleavage sites in protein sequences","volume":"33","author":"Backes","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1093\/bioinformatics\/btt603","article-title":"Cascleave 2.0, a new approach for predicting caspase and granzyme cleavage targets","volume":"30","author":"Wang","year":"2014","journal-title":"Bioinformatics"},{"key":"ref_69","first-page":"3191","article-title":"The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability","volume":"17","author":"Nakazawa","year":"2011","journal-title":"Mol. Vis."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"183660","DOI":"10.1016\/j.bbamem.2021.183660","article-title":"Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms","volume":"1863","author":"Robustelli","year":"2021","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"291","DOI":"10.3389\/fcell.2019.00291","article-title":"Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission","volume":"7","author":"Zhukovsky","year":"2019","journal-title":"Front. Cell. Dev. Biol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"19426","DOI":"10.1074\/jbc.M602203200","article-title":"Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase","volume":"281","author":"Higgins","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"167774","DOI":"10.1016\/j.jmb.2022.167774","article-title":"Complexin Membrane Interactions: Implications for Synapse Evolution and Function","volume":"435","author":"Lottermoser","year":"2023","journal-title":"J. Mol. Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1007\/s00439-006-0319-6","article-title":"Autosomal recessive juvenile onset cataract associated with mutation in BFSP1","volume":"121","author":"Ramachandran","year":"2007","journal-title":"Hum. Genet."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1194\/jlr.R004119","article-title":"Lipids and the ocular lens","volume":"51","author":"Borchman","year":"2010","journal-title":"J. Lipid Res."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Costello, M.J., Brennan, L.A., Mohamed, A., Gilliland, K.O., Johnsen, S., and Kantorow, M. (2016). Identification and Ultrastructural Characterization of a Novel Nuclear Degradation Complex in Differentiating Lens Fiber Cells. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0160785"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/exer.2001.1111","article-title":"Lens organelle degradation","volume":"74","author":"Bassnett","year":"2002","journal-title":"Exp. Eye Res."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1167\/iovs.63.8.5","article-title":"Lens Aquaporin-5 Inserts into Bovine Fiber Cell Plasma Membranes via Unconventional Protein Secretion","volume":"63","author":"Gletten","year":"2022","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.exer.2016.03.009","article-title":"The cause and consequence of fiber cell compaction in the vertebrate lens","volume":"156","author":"Bassnett","year":"2017","journal-title":"Exp. Eye Res."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1242\/jcs.045203","article-title":"The stratified syncytium of the vertebrate lens","volume":"122","author":"Shi","year":"2009","journal-title":"J. Cell. Sci."},{"key":"ref_81","first-page":"970","article-title":"Expression of the type VI intermediate filament proteins CP49 and filensin in the mouse lens epithelium","volume":"22","author":"FitzGerald","year":"2016","journal-title":"Mol. Vis."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1167\/iovs.08-2894","article-title":"Periplakin Serves as a Linker for Both Vimentin and the Highly Divergent Beaded Filament Proteins in the Ocular Lens","volume":"50","author":"Yoon","year":"2008","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"4985","DOI":"10.1242\/jcs.00815","article-title":"A novel cell-cell junction system: The cortex adhaerens mosaic of lens fiber cells","volume":"116","author":"Straub","year":"2003","journal-title":"J. Cell. Sci."},{"key":"ref_84","first-page":"301","article-title":"Plakoglobin is a component of the filamentous subplasmalemmal coat of lens cells","volume":"43","author":"Franke","year":"1987","journal-title":"Eur. J. Cell. Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1242\/jcs.202168","article-title":"A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks","volume":"130","author":"Quinlan","year":"2017","journal-title":"J. Cell. Sci."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"e2000078","DOI":"10.1002\/bies.202000078","article-title":"Mechanical and Non-Mechanical Functions of Filamentous and Non-Filamentous Vimentin","volume":"42","author":"Patteson","year":"2020","journal-title":"Bioessays"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e2105640","DOI":"10.1002\/smll.202105640","article-title":"Extracellular Vimentin as a Target against SARS-CoV-2 Host Cell Invasion","volume":"18","author":"Suprewicz","year":"2022","journal-title":"Small"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/12\/1580\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T19:50:07Z","timestamp":1760125807000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/12\/1580"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,6,7]]},"references-count":87,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2023,6]]}},"alternative-id":["cells12121580"],"URL":"https:\/\/doi.org\/10.3390\/cells12121580","relation":{},"ISSN":["2073-4409"],"issn-type":[{"type":"electronic","value":"2073-4409"}],"subject":[],"published":{"date-parts":[[2023,6,7]]}}}