{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T17:54:08Z","timestamp":1777312448572,"version":"3.51.4"},"reference-count":56,"publisher":"The Company of Biologists","issue":"12","license":[{"start":{"date-parts":[[2023,6,15]],"date-time":"2023-06-15T00:00:00Z","timestamp":1686787200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R15GM134496"],"award-info":[{"award-number":["R15GM134496"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01GM144652"],"award-info":[{"award-number":["R01GM144652"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"name":"National Science Foundation","award":["2144701"],"award-info":[{"award-number":["2144701"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Polycystins are a family of conserved ion channels, mutations of which lead to one of the most common human genetic disorders, namely, autosomal dominant polycystic kidney disease. Schizosacchromyces pombe possesses an essential polycystin homologue, Pkd2, which directs Ca2+ influx on the cell surface in response to membrane tension, but its structure remains unsolved. Here, we analyzed the structure\u2013function relationship of Pkd2 based on its AlphaFold-predicted structure. Pkd2 consists of three domains, the extracellular lipid-binding domain (LBD), nine-helix transmembrane domain (TMD) and C-terminal cytoplasmic domain (CCD). Our genetic and microscopy data revealed that LBD and TMD are essential for targeting Pkd2 to the plasma membrane from the endoplasmic reticulum. In comparison, CCD ensures the polarized distribution of Pkd2 by promoting its internalization and preventing its clustering in the eisosome, a caveolae-like membrane compartment. The domains of Pkd2 and their functions are conserved in other fission yeast species. We conclude that both extracellular and cytoplasmic domains of Pkd2 are crucial for its intracellular trafficking and function. We propose that mechanosensitive channels can be desensitized through either internalization or clustering in low-tension membrane compartments.<\/jats:p>","DOI":"10.1242\/jcs.260598","type":"journal-article","created":{"date-parts":[[2023,6,1]],"date-time":"2023-06-01T09:04:46Z","timestamp":1685610286000},"source":"Crossref","is-referenced-by-count":10,"title":["The cytoplasmic tail of the mechanosensitive channel Pkd2 regulates its internalization and clustering in eisosomes"],"prefix":"10.1242","volume":"136","author":[{"given":"Mamata","family":"Malla","sequence":"first","affiliation":[{"name":"The University of Toledo Department of Biological Sciences , , 2801 West Bancroft Street, Toledo, OH 43606 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Debatrayee","family":"Sinha","sequence":"additional","affiliation":[{"name":"The University of Toledo Department of Biological Sciences , , 2801 West Bancroft Street, Toledo, OH 43606 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pritha","family":"Chowdhury","sequence":"additional","affiliation":[{"name":"The University of Toledo Department of Biological Sciences , , 2801 West Bancroft Street, Toledo, OH 43606 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Benjamin Thomas","family":"Bisesi","sequence":"additional","affiliation":[{"name":"The University of Toledo Department of Biological Sciences , , 2801 West Bancroft Street, Toledo, OH 43606 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2768-6570","authenticated-orcid":false,"given":"Qian","family":"Chen","sequence":"additional","affiliation":[{"name":"The University of Toledo Department of Biological Sciences , , 2801 West Bancroft Street, Toledo, OH 43606 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[2023,6,27]]},"reference":[{"key":"2023062808345186100_JCS260598C1","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1091\/mbc.E19-04-0218","article-title":"Plasma membrane tension regulates eisosome structure and function","volume":"31","author":"Appadurai","year":"2020","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C2","doi-asserted-by":"publisher","first-page":"943","DOI":"10.1002\/(SICI)1097-0061(199807)14:10&lt;943::AID-YEA292&gt;3.0.CO;2-Y","article-title":"Heterologous modules for efficient and versatile PCR\u2013based gene targeting in Schizosaccharomyces pombe","volume":"14","author":"B\u00e4hler","year":"1998","journal-title":"Yeast"},{"key":"2023062808345186100_JCS260598C3","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1038\/s41467-018-02864-2","article-title":"Steric exclusion and protein conformation determine the localization of plasma membrane transporters","volume":"9","author":"Bianchi","year":"2018","journal-title":"Nat. Commun."},{"key":"2023062808345186100_JCS260598C4","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1006\/jmbi.1994.1582","article-title":"The immunoglobulin fold. Structural classification, sequence patterns and common core","volume":"242","author":"Bork","year":"1994","journal-title":"J. Mol. Biol."},{"key":"2023062808345186100_JCS260598C5","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1093\/hmg\/4.4.575","article-title":"Analysis of the genomic sequence for the autosomal dominant polycystic kidney disease (PKD1) gene predicts the presence of a leucine-rich repeat. The American PKD1 Consortium (APKD1 Consortium)","volume":"4","author":"Burn","year":"1995","journal-title":"Hum. Mol. Genet."},{"key":"2023062808345186100_JCS260598C6","doi-asserted-by":"publisher","first-page":"28557","DOI":"10.1074\/jbc.274.40.28557","article-title":"Identification and characterization of polycystin-2, the PKD2 gene product","volume":"274","author":"Cai","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2023062808345186100_JCS260598C7","doi-asserted-by":"publisher","first-page":"814","DOI":"10.1681\/ASN.V115814","article-title":"Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene","volume":"11","author":"Foggensteiner","year":"2000","journal-title":"J. Am. Soc. Nephrol."},{"key":"2023062808345186100_JCS260598C8","doi-asserted-by":"publisher","first-page":"2512","DOI":"10.1073\/pnas.0437840100","article-title":"Structure of a cholesterol-binding protein deficient in Niemann\u2013Pick type C2 disease","volume":"100","author":"Friedland","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023062808345186100_JCS260598C9","doi-asserted-by":"publisher","first-page":"2674","DOI":"10.1172\/JCI119090","article-title":"Identification and localization of polycystin, the PKD1 gene product","volume":"98","author":"Geng","year":"1996","journal-title":"J. Clin. Invest."},{"key":"2023062808345186100_JCS260598C10","doi-asserted-by":"publisher","first-page":"E3145","DOI":"10.1073\/pnas.1719462115","article-title":"Conformation-dependent partitioning of yeast nutrient transporters into starvation-protective membrane domains","volume":"115","author":"Gournas","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2023062808345186100_JCS260598C11","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1038\/nsmb.3343","article-title":"Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2)","volume":"24","author":"Grieben","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2023062808345186100_JCS260598C12","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/sj.emboj.7601466","article-title":"Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast","volume":"26","author":"Grossmann","year":"2007","journal-title":"EMBO J."},{"key":"2023062808345186100_JCS260598C13","doi-asserted-by":"publisher","first-page":"1075","DOI":"10.1083\/jcb.200806035","article-title":"Plasma membrane microdomains regulate turnover of transport proteins in yeast","volume":"183","author":"Grossmann","year":"2008","journal-title":"J. Cell Biol."},{"key":"2023062808345186100_JCS260598C14","doi-asserted-by":"publisher","first-page":"278","DOI":"10.1681\/ASN.2008060564","article-title":"Characterization of PKD protein-positive exosome-like vesicles","volume":"20","author":"Hogan","year":"2009","journal-title":"J. Am. Soc. Nephrol."},{"key":"2023062808345186100_JCS260598C15","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1534\/genetics.116.193458","article-title":"Traffic through the trans-Golgi network and the endosomal system requires collaboration between exomer and clathrin adaptors in fission yeast","volume":"205","author":"Hoya","year":"2017","journal-title":"Genetics"},{"key":"2023062808345186100_JCS260598C16","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1007\/s00239-004-0218-1","article-title":"Comparison of the yeast proteome to other fungal genomes to find core fungal genes","volume":"60","author":"Hsiang","year":"2005","journal-title":"J. Mol. Evol."},{"key":"2023062808345186100_JCS260598C17","doi-asserted-by":"publisher","first-page":"356","DOI":"10.1074\/jbc.273.1.356","article-title":"Solution structure of Der f 2, the major mite allergen for atopic diseases","volume":"273","author":"Ichikawa","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2023062808345186100_JCS260598C18","doi-asserted-by":"publisher","first-page":"1208","DOI":"10.1016\/j.febslet.2004.11.115","article-title":"Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity","volume":"579","author":"Johannessen","year":"2005","journal-title":"FEBS Lett."},{"key":"2023062808345186100_JCS260598C19","doi-asserted-by":"publisher","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":"2023062808345186100_JCS260598C20","doi-asserted-by":"publisher","first-page":"4059","DOI":"10.1091\/mbc.e11-07-0605","article-title":"The filament-forming protein Pil1 assembles linear eisosomes in fission yeast","volume":"22","author":"Kabeche","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C21","doi-asserted-by":"publisher","first-page":"4057","DOI":"10.1242\/jcs.176867","article-title":"Eisosomes provide membrane reservoirs for rapid expansion of the yeast plasma membrane","volume":"128","author":"Kabeche","year":"2015","journal-title":"J. Cell Sci."},{"key":"2023062808345186100_JCS260598C23","doi-asserted-by":"publisher","first-page":"e62084","DOI":"10.7554\/eLife.62084","article-title":"Rapid adaptation of endocytosis, exocytosis, and eisosomes after an acute increase in membrane tension in yeast cells","volume":"10","author":"Lemi\u00e8re","year":"2021","journal-title":"Elife"},{"key":"2023062808345186100_JCS260598C24","doi-asserted-by":"publisher","first-page":"e33183","DOI":"10.7554\/eLife.33183","article-title":"Polycystin-2 is an essential ion channel subunit in the primary cilium of the renal collecting duct epithelium","volume":"7","author":"Liu","year":"2018","journal-title":"Elife"},{"key":"2023062808345186100_JCS260598C25","doi-asserted-by":"publisher","first-page":"4427","DOI":"10.1091\/mbc.e03-04-0221","article-title":"Visualization of protein compartmentation within the plasma membrane of living yeast cells","volume":"14","author":"Malinska","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C26","doi-asserted-by":"publisher","first-page":"1129","DOI":"10.1016\/j.devcel.2012.11.004","article-title":"ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology","volume":"23","author":"Manford","year":"2012","journal-title":"Dev. Cell"},{"key":"2023062808345186100_JCS260598C27","doi-asserted-by":"publisher","first-page":"e202001147","DOI":"10.1083\/jcb.202001147","article-title":"Sterol biosensor reveals LAM-family Ltc1-dependent sterol flow to endosomes upon Arp2\/3 inhibition","volume":"219","author":"Marek","year":"2020","journal-title":"J. Cell Biol."},{"key":"2023062808345186100_JCS260598C28","doi-asserted-by":"publisher","first-page":"1339","DOI":"10.1126\/science.272.5266.1339","article-title":"PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein","volume":"272","author":"Mochizuki","year":"1996","journal-title":"Science."},{"key":"2023062808345186100_JCS260598C29","doi-asserted-by":"publisher","first-page":"2113","DOI":"10.1091\/mbc.E17-11-0691","article-title":"Eisosomes are metabolically regulated storage compartments for APC-type nutrient transporters","volume":"29","author":"Moharir","year":"2018","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C30","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1016\/0076-6879(91)94059-L","article-title":"Molecular genetic analysis of fission yeast Schizosaccharomyces pombe","volume":"194","author":"Moreno","year":"1991","journal-title":"Methods Enzymol."},{"key":"2023062808345186100_JCS260598C31","doi-asserted-by":"publisher","first-page":"1791","DOI":"10.1091\/mbc.E18-04-0270","article-title":"Fission yeast TRP channel Pkd2p localizes to the cleavage furrow and regulates cell separation during cytokinesis","volume":"30","author":"Morris","year":"2019","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C32","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1091\/mbc.10.3.799","article-title":"Visualization of receptor-mediated endocytosis in yeast","volume":"10","author":"Mulholland","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C33","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1038\/ng1076","article-title":"Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells","volume":"33","author":"Nauli","year":"2003","journal-title":"Nat. Genet."},{"key":"2023062808345186100_JCS260598C34","doi-asserted-by":"publisher","first-page":"1434","DOI":"10.1016\/j.celrep.2019.12.098","article-title":"Plasma membrane furrows control plasticity of ER-PM contacts","volume":"30","author":"Ng","year":"2020","journal-title":"Cell Reports"},{"key":"2023062808345186100_JCS260598C35","doi-asserted-by":"publisher","first-page":"884","DOI":"10.1093\/bioinformatics\/btt607","article-title":"Protter: interactive protein feature visualization and integration with experimental proteomic data","volume":"30","author":"Omasits","year":"2014","journal-title":"Bioinformatics"},{"key":"2023062808345186100_JCS260598C36","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1042\/BJ20041710","article-title":"A microbial TRP-like polycystic-kidney-disease-related ion channel gene","volume":"387","author":"Palmer","year":"2005","journal-title":"Biochem. J."},{"key":"2023062808345186100_JCS260598C37","doi-asserted-by":"publisher","first-page":"3313","DOI":"10.1093\/hmg\/ddy223","article-title":"A mutation affecting polycystin-1 mediated heterotrimeric G-protein signaling causes PKD","volume":"27","author":"Parnell","year":"2018","journal-title":"Hum. Mol. Genet."},{"key":"2023062808345186100_JCS260598C38","doi-asserted-by":"publisher","first-page":"R378","DOI":"10.1016\/S0960-9822(02)00877-1","article-title":"Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease","volume":"12","author":"Pazour","year":"2002","journal-title":"Curr. Biol."},{"key":"2023062808345186100_JCS260598C39","doi-asserted-by":"publisher","first-page":"938","DOI":"10.1016\/S0960-9822(02)00869-2","article-title":"The ion channel polycystin-2 is required for left-right axis determination in mice","volume":"12","author":"Pennekamp","year":"2002","journal-title":"Curr. Biol."},{"key":"2023062808345186100_JCS260598C60","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera - a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"2023062808345186100_JCS260598C40","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1091\/mbc.E20-09-0609","article-title":"Calcium spikes accompany cleavage furrow ingression and cell separation during fission yeast cytokinesis","volume":"32","author":"Poddar","year":"2021","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C41","doi-asserted-by":"publisher","first-page":"ar134","DOI":"10.1091\/mbc.E22-07-0248","article-title":"Membrane stretching activates calcium-permeability of a putative channel Pkd2 during fission yeast cytokinesis","volume":"33","author":"Poddar","year":"2022","journal-title":"Mol. Biol. Cell"},{"key":"2023062808345186100_JCS260598C42","doi-asserted-by":"publisher","first-page":"16981","DOI":"10.1073\/pnas.252484899","article-title":"Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations","volume":"99","author":"Qian","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2023062808345186100_JCS260598C43","doi-asserted-by":"publisher","first-page":"930","DOI":"10.1126\/science.1203357","article-title":"Comparative functional genomics of the fission yeasts","volume":"332","author":"Rhind","year":"2011","journal-title":"Science"},{"key":"2023062808345186100_JCS260598C44","doi-asserted-by":"publisher","first-page":"1116","DOI":"10.1085\/jgp.201912327","article-title":"A stochastic model of ion channel cluster formation in the plasma membrane","volume":"151","author":"Sato","year":"2019","journal-title":"J. Gen. Physiol."},{"key":"2023062808345186100_JCS260598C45","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1016\/j.cell.2016.09.048","article-title":"The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs","volume":"167","author":"Shen","year":"2016","journal-title":"Cell"},{"key":"2023062808345186100_JCS260598C46","doi-asserted-by":"publisher","first-page":"jcs259046","DOI":"10.1242\/jcs.259046","article-title":"Fission yeast polycystin Pkd2p promotes cell size expansion and antagonizes the Hippo-related SIN pathway","volume":"135","author":"Sinha","year":"2022","journal-title":"J. Cell Sci."},{"key":"2023062808345186100_JCS260598C47","doi-asserted-by":"publisher","first-page":"4063","DOI":"10.1242\/jcs.160556","article-title":"Regulation of polycystin-1 ciliary trafficking by motifs at its C-terminus and polycystin-2 but not by cleavage at the GPS site","volume":"128","author":"Su","year":"2015","journal-title":"J. Cell Sci."},{"key":"2023062808345186100_JCS260598C48","doi-asserted-by":"publisher","first-page":"eaat9819","DOI":"10.1126\/science.aat9819","article-title":"Structure of the human PKD1-PKD2 complex","volume":"361","author":"Su","year":"2018","journal-title":"Science"},{"key":"2023062808345186100_JCS260598C49","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1038\/s41587-021-01156-3","article-title":"SignalP 6.0 predicts all five types of signal peptides using protein language models","volume":"40","author":"Teufel","year":"2022","journal-title":"Nat. Biotechnol."},{"key":"2023062808345186100_JCS260598C50","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1109\/83.650848","article-title":"A pyramid approach to subpixel registration based on intensity","volume":"7","author":"Thevenaz","year":"1998","journal-title":"IEEE Trans. Image Process."},{"key":"2023062808345186100_JCS260598C51","doi-asserted-by":"publisher","first-page":"jcs240754","DOI":"10.1242\/jcs.240754","article-title":"A toolbox of stable integration vectors in the fission yeast Schizosaccharomyces pombe","volume":"133","author":"Vje\u0161tica","year":"2020","journal-title":"J. Cell Sci."},{"key":"2023062808345186100_JCS260598C52","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.cub.2014.01.002","article-title":"C. elegans ciliated sensory neurons release extracellular vesicles that function in animal communication","volume":"24","author":"Wang","year":"2014","journal-title":"Curr. Biol."},{"key":"2023062808345186100_JCS260598C53","doi-asserted-by":"publisher","first-page":"e1002437","DOI":"10.1371\/journal.pbio.1002437","article-title":"Roles of the TRAPP-II complex and the exocyst in membrane deposition during fission yeast cytokinesis","volume":"14","author":"Wang","year":"2016","journal-title":"PLoS Biol."},{"key":"2023062808345186100_JCS260598C54","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1038\/nsmb.3357","article-title":"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2","volume":"24","author":"Wilkes","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2023062808345186100_JCS260598C55","doi-asserted-by":"publisher","first-page":"927","DOI":"10.1128\/MCB.22.3.927-934.2002","article-title":"The Sur7p family defines novel cortical domains in Saccharomyces cerevisiae, affects sphingolipid metabolism, and is involved in sporulation","volume":"22","author":"Young","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"2023062808345186100_JCS260598C56","doi-asserted-by":"publisher","first-page":"2048","DOI":"10.1016\/j.cub.2012.08.047","article-title":"Plasma membrane tethering of the cortical ER necessitates its finely reticulated architecture","volume":"22","author":"Zhang","year":"2012","journal-title":"Curr. Biol."}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.260598\/2898544\/jcs260598.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.260598\/2992861\/jcs260598.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.260598\/2992861\/jcs260598.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,6,28]],"date-time":"2023-06-28T08:35:01Z","timestamp":1687941301000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/136\/12\/jcs260598\/319902\/The-cytoplasmic-tail-of-the-mechanosensitive"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,6,15]]},"references-count":56,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2023,6,15]]}},"URL":"https:\/\/doi.org\/10.1242\/jcs.260598","relation":{},"ISSN":["0021-9533","1477-9137"],"issn-type":[{"value":"0021-9533","type":"print"},{"value":"1477-9137","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,6,15]]},"article-number":"jcs260598"}}