{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T09:36:36Z","timestamp":1793957796423,"version":"4.8.0"},"reference-count":78,"publisher":"American Society of Hematology","issue":"4","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2024,1,25]]},"abstract":"<jats:sec>\n                    <jats:title>Abstract<\/jats:title>\n                    <jats:p>Cell-surface exposure of phosphatidylserine (PS) is essential for phagocytic clearance and blood clotting. Although a calcium-activated phospholipid scramblase (CaPLSase) has long\u00a0been proposed to mediate PS exposure in red blood cells (RBCs), its identity, activation mechanism, and role in RBC biology and disease remain elusive. Here, we demonstrate that TMEM16F, the long-sought-after RBC CaPLSase, is activated by calcium influx through the mechanosensitive channel PIEZO1 in RBCs. PIEZO1-TMEM16F functional coupling is enhanced in RBCs from individuals with hereditary xerocytosis (HX), an RBC disorder caused by PIEZO1 gain-of-function channelopathy. Enhanced PIEZO1-TMEM16F coupling leads to an increased propensity to expose PS, which may serve as a key risk factor for HX clinical manifestations including anemia, splenomegaly, and postsplenectomy thrombosis. Spider toxin GsMTx-4 and antigout medication benzbromarone inhibit PIEZO1, preventing force-induced echinocytosis, hemolysis, and PS exposure in HX RBCs. Our study thus reveals an activation mechanism of TMEM16F CaPLSase and its pathophysiological function in HX, providing insights into potential treatment.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1182\/blood.2023021465","type":"journal-article","created":{"date-parts":[[2023,11,30]],"date-time":"2023-11-30T16:11:05Z","timestamp":1701360665000},"page":"357-369","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":51,"title":["Deciphering and disrupting PIEZO1-TMEM16F interplay in hereditary xerocytosis"],"prefix":"10.1182","volume":"143","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5128-1509","authenticated-orcid":false,"given":"Pengfei","family":"Liang","sequence":"first","affiliation":[{"name":"1Department of Biochemistry, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3625-9965","authenticated-orcid":false,"given":"Yang","family":"Zhang","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3189-0021","authenticated-orcid":false,"given":"Yui Chun S.","family":"Wan","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shang","family":"Ma","sequence":"additional","affiliation":[{"name":"2Children\u2019s Research Institute, UT Southwestern Medical Center, Dallas, TX"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6640-6607","authenticated-orcid":false,"given":"Ping","family":"Dong","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Augustus J.","family":"Lowry","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3210-0789","authenticated-orcid":false,"given":"Samuel J.","family":"Francis","sequence":"additional","affiliation":[{"name":"3Department of Surgery, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5661-3856","authenticated-orcid":false,"given":"Sanjay","family":"Khandelwal","sequence":"additional","affiliation":[{"name":"4Department of Medicine, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martha","family":"Delahunty","sequence":"additional","affiliation":[{"name":"4Department of Medicine, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3809-1780","authenticated-orcid":false,"given":"Marilyn J.","family":"Telen","sequence":"additional","affiliation":[{"name":"4Department of Medicine, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0341-1457","authenticated-orcid":false,"given":"John J.","family":"Strouse","sequence":"additional","affiliation":[{"name":"4Department of Medicine, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gowthami M.","family":"Arepally","sequence":"additional","affiliation":[{"name":"4Department of Medicine, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9521-9328","authenticated-orcid":false,"given":"Huanghe","family":"Yang","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry, Duke University School of Medicine, Durham, NC"},{"name":"5Department of Neurobiology, Duke University School of Medicine, Durham, NC"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"234","reference":[{"issue":"1","key":"2024012516213707600_bib1","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1146\/annurev.biophys.093008.131234","article-title":"The distribution and function of phosphatidylserine in cellular membranes","volume":"39","author":"Leventis","year":"2010","journal-title":"Annu Rev Biophys"},{"issue":"2","key":"2024012516213707600_bib2","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1152\/physrev.00020.2015","article-title":"Getting to the outer leaflet: physiology of phosphatidylserine exposure at the plasma membrane","volume":"96","author":"Bevers","year":"2016","journal-title":"Physiol Rev"},{"issue":"8","key":"2024012516213707600_bib3","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1038\/s41580-023-00604-z","article-title":"Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases","volume":"24","author":"Sakuragi","year":"2023","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024012516213707600_bib4","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/978-94-007-6331-9_10","article-title":"Phosphatidylserine-mediated cellular signaling","volume":"991","author":"Kay","year":"2013","journal-title":"Adv Exp Med Biol"},{"issue":"2","key":"2024012516213707600_bib5","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/sj.cdd.4400473","article-title":"Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages","volume":"6","author":"Krahling","year":"1999","journal-title":"Cell Death Differ"},{"issue":"2","key":"2024012516213707600_bib6","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1006\/bbrc.1998.8663","article-title":"Essential role of phosphatidylserine externalization in apoptosing cell phagocytosis by macrophages","volume":"246","author":"Shiratsuchi","year":"1998","journal-title":"Biochem Biophys Res Commun"},{"issue":"11","key":"2024012516213707600_bib7","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.tcb.2015.08.003","article-title":"An apoptotic 'Eat Me' signal: phosphatidylserine exposure","volume":"25","author":"Segawa","year":"2015","journal-title":"Trends Cell Biol"},{"issue":"5","key":"2024012516213707600_bib8","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/S0163-7827(03)00025-0","article-title":"Exposure of platelet membrane phosphatidylserine regulates blood coagulation","volume":"42","author":"Lentz","year":"2003","journal-title":"Prog Lipid Res"},{"issue":"1","key":"2024012516213707600_bib9","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1074\/jbc.M117.809681","article-title":"Cell-surface phosphatidylserine regulates osteoclast precursor fusion","volume":"293","author":"Verma","year":"2018","journal-title":"J\u00a0Biol Chem"},{"issue":"38","key":"2024012516213707600_bib10","doi-asserted-by":"crossref","first-page":"e2202490119","DOI":"10.1073\/pnas.2202490119","article-title":"Phosphatidylserine orchestrates Myomerger membrane insertions to drive myoblast fusion","volume":"119","author":"Gamage","year":"2022","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"2024012516213707600_bib11","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.chom.2017.06.012","article-title":"Fusion stage of HIV-1 entry depends on virus-induced cell surface exposure of phosphatidylserine","volume":"22","author":"Zaitseva","year":"2017","journal-title":"Cell Host Microbe"},{"issue":"3","key":"2024012516213707600_bib12","doi-asserted-by":"crossref","first-page":"e1003232","DOI":"10.1371\/journal.ppat.1003232","article-title":"TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine","volume":"9","author":"Jemielity","year":"2013","journal-title":"PLoS Pathog"},{"issue":"19","key":"2024012516213707600_bib13","doi-asserted-by":"crossref","first-page":"eaba0310","DOI":"10.1126\/sciadv.aba0310","article-title":"TMEM16F phospholipid scramblase mediates trophoblast fusion and placental development","volume":"6","author":"Zhang","year":"2020","journal-title":"Sci Adv"},{"issue":"5","key":"2024012516213707600_bib14","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1083\/jcb.201901017","article-title":"How cells fuse","volume":"218","author":"Brukman","year":"2019","journal-title":"J\u00a0Cell Biol"},{"issue":"5","key":"2024012516213707600_bib15","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1111\/j.1538-7836.2011.04251.x","article-title":"Red blood cell phosphatidylserine exposure is responsible for increased erythrocyte adhesion to endothelium in central retinal vein occlusion","volume":"9","author":"Wautier","year":"2011","journal-title":"J\u00a0Thromb Haemost"},{"issue":"9","key":"2024012516213707600_bib16","first-page":"00009","article-title":"Of macrophages and red blood cells; a complex love story","volume":"5","author":"de Back","year":"2014","journal-title":"Front Physiol"},{"issue":"2","key":"2024012516213707600_bib17","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1046\/j.1365-2141.1999.01718.x","article-title":"Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium","volume":"107","author":"Closse","year":"1999","journal-title":"Br J Haematol"},{"issue":"4","key":"2024012516213707600_bib18","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/S0272-6386(01)80130-X","article-title":"Involvement of phosphatidylserine exposure in the recognition and phagocytosis of uremic erythrocytes","volume":"37","author":"Bonomini","year":"2001","journal-title":"Am J Kidney Dis"},{"issue":"5","key":"2024012516213707600_bib19","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/j.thromres.2013.01.023","article-title":"The role of the red cell membrane in thrombin generation","volume":"131","author":"Whelihan","year":"2013","journal-title":"Thromb Res"},{"issue":"18","key":"2024012516213707600_bib20","doi-asserted-by":"crossref","first-page":"3837","DOI":"10.1182\/blood-2012-05-427856","article-title":"Prothrombin activation in blood coagulation: the erythrocyte contribution to thrombin generation","volume":"120","author":"Whelihan","year":"2012","journal-title":"Blood"},{"issue":"5","key":"2024012516213707600_bib21","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1159\/000086406","article-title":"Mechanisms of suicidal erythrocyte death","volume":"15","author":"Lang","year":"2005","journal-title":"Cell Physiol Biochem"},{"issue":"2","key":"2024012516213707600_bib22","first-page":"147","article-title":"The role of phosphatidylserine in recognition and removal of erythrocytes","volume":"50","author":"Kuypers","year":"2004","journal-title":"Cell Mol Biol"},{"issue":"7325","key":"2024012516213707600_bib23","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1038\/nature09583","article-title":"Calcium-dependent phospholipid scrambling by TMEM16F","volume":"468","author":"Suzuki","year":"2010","journal-title":"Nature"},{"issue":"27","key":"2024012516213707600_bib24","doi-asserted-by":"crossref","first-page":"6355","DOI":"10.1021\/bi00142a027","article-title":"Ca2+ induces transbilayer redistribution of all major phospholipids in human erythrocytes","volume":"31","author":"Williamson","year":"1992","journal-title":"Biochemistry"},{"issue":"2","key":"2024012516213707600_bib25","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/0005-2736(90)90058-V","article-title":"Loss of membrane phospholipid asymmetry in platelets and red cells may be associated with calcium-induced shedding of plasma membrane and inhibition of aminophospholipid translocase","volume":"1026","author":"Comfurius","year":"1990","journal-title":"Biochim Biophys Acta"},{"issue":"2","key":"2024012516213707600_bib26","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1182\/blood.V79.2.380.380","article-title":"Defective Ca(2+)-induced microvesiculation and deficient expression of procoagulant activity in erythrocytes from a patient with a bleeding disorder: a study of the red blood cells of Scott syndrome","volume":"79","author":"Bevers","year":"1992","journal-title":"Blood"},{"issue":"1","key":"2024012516213707600_bib27","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.cell.2012.07.036","article-title":"TMEM16F forms a Ca2+-activated cation channel required for lipid scrambling in platelets during blood coagulation","volume":"151","author":"Yang","year":"2012","journal-title":"Cell"},{"issue":"41","key":"2024012516213707600_bib28","doi-asserted-by":"crossref","first-page":"12800","DOI":"10.1073\/pnas.1516594112","article-title":"TMEM16F is required for phosphatidylserine exposure and microparticle release in activated mouse platelets","volume":"112","author":"Fujii","year":"2015","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"2024012516213707600_bib29","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.celrep.2019.06.023","article-title":"Cryo-EM studies of TMEM16F calcium-activated ion channel suggest features important for lipid scrambling","volume":"28","author":"Feng","year":"2019","journal-title":"Cell Rep"},{"key":"2024012516213707600_bib30","doi-asserted-by":"crossref","first-page":"e44365","DOI":"10.7554\/eLife.44365","article-title":"Cryo-EM structures and functional characterization of the murine lipid scramblase TMEM16F","volume":"8","author":"Alvadia","year":"2019","journal-title":"Elife"},{"key":"2024012516213707600_bib31","doi-asserted-by":"crossref","first-page":"e06901","DOI":"10.7554\/eLife.06901","article-title":"Identification of a lipid scrambling domain in ANO6\/TMEM16F","volume":"4","author":"Yu","year":"2015","journal-title":"Elife"},{"issue":"2-3","key":"2024012516213707600_bib32","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.bbalip.2003.07.003","article-title":"Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids","volume":"1636","author":"Zwaal","year":"2004","journal-title":"Biochim Biophys Acta"},{"key":"2024012516213707600_bib33","doi-asserted-by":"crossref","first-page":"e07370","DOI":"10.7554\/eLife.07370","article-title":"Piezo1 links mechanical forces to red blood cell volume","volume":"4","author":"Cahalan","year":"2015","journal-title":"Elife"},{"issue":"1","key":"2024012516213707600_bib34","doi-asserted-by":"crossref","first-page":"E9","DOI":"10.1002\/ajh.24923","article-title":"Revised prevalence estimate of possible hereditary xerocytosis as derived from a large US Laboratory database","volume":"93","author":"Kaufman","year":"2018","journal-title":"Am J Hematol"},{"issue":"25","key":"2024012516213707600_bib35","doi-asserted-by":"crossref","first-page":"2699","DOI":"10.1182\/blood-2017-04-590810","article-title":"Disorders of erythrocyte hydration","volume":"130","author":"Gallagher","year":"2017","journal-title":"Blood"},{"issue":"8","key":"2024012516213707600_bib36","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1002\/ajh.26192","article-title":"Recent advances in the pathophysiology of PIEZO1-related hereditary xerocytosis","volume":"96","author":"Jankovsky","year":"2021","journal-title":"Am J Hematol"},{"issue":"9","key":"2024012516213707600_bib37","doi-asserted-by":"crossref","first-page":"1908","DOI":"10.1182\/blood-2012-04-422253","article-title":"Mutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis","volume":"120","author":"Zarychanski","year":"2012","journal-title":"Blood"},{"key":"2024012516213707600_bib38","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1038\/ncomms2899","article-title":"Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels","volume":"4","author":"Albuisson","year":"2013","journal-title":"Nat Commun"},{"issue":"6","key":"2024012516213707600_bib39","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1113\/JP275718","article-title":"Human phenotypes caused by PIEZO1 mutations; one gene, two overlapping phenotypes?","volume":"596","author":"Martin-Almedina","year":"2018","journal-title":"J\u00a0Physiol"},{"issue":"3","key":"2024012516213707600_bib40","doi-asserted-by":"crossref","first-page":"e94","DOI":"10.3324\/haematol.2017.180687","article-title":"PIEZO1-R1864H rare variant accounts for a genetic phenotype-modifier role in dehydrated hereditary stomatocytosis","volume":"103","author":"Andolfo","year":"2018","journal-title":"Haematologica"},{"issue":"11","key":"2024012516213707600_bib41","doi-asserted-by":"crossref","first-page":"1284","DOI":"10.3324\/haematol.2016.142463","article-title":"New insights on hereditary erythrocyte membrane defects","volume":"101","author":"Andolfo","year":"2016","journal-title":"Haematologica"},{"issue":"19","key":"2024012516213707600_bib42","doi-asserted-by":"crossref","first-page":"3925","DOI":"10.1182\/blood-2013-02-482489","article-title":"Multiple clinical forms of dehydrated hereditary stomatocytosis arise from mutations in PIEZO1","volume":"121","author":"Andolfo","year":"2013","journal-title":"Blood"},{"issue":"12","key":"2024012516213707600_bib43","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1002\/ajh.23799","article-title":"Hereditary xerocytosis revisited","volume":"89","author":"Archer","year":"2014","journal-title":"Am J Hematol"},{"issue":"16","key":"2024012516213707600_bib44","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1182\/blood-2017-05-786004","article-title":"Novel mechanisms of PIEZO1 dysfunction in hereditary xerocytosis","volume":"130","author":"Glogowska","year":"2017","journal-title":"Blood"},{"key":"2024012516213707600_bib45","doi-asserted-by":"crossref","first-page":"102413","DOI":"10.1016\/j.bcmd.2020.102413","article-title":"Heterogeneous phenotype of hereditary xerocytosis in association with PIEZO1 variants","volume":"82","author":"de Meira Oliveira","year":"2020","journal-title":"Blood Cells Mol Dis"},{"issue":"8","key":"2024012516213707600_bib46","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.3324\/haematol.2018.205328","article-title":"Clinical and biological features in PIEZO1-hereditary xerocytosis and gardos channelopathy: a retrospective series of 126 patients","volume":"104","author":"Picard","year":"2019","journal-title":"Haematologica"},{"issue":"3","key":"2024012516213707600_bib47","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1086\/302024","article-title":"Genomewide search for dehydrated hereditary stomatocytosis (hereditary xerocytosis): mapping of locus to chromosome 16 (16q23-qter)","volume":"63","author":"Carella","year":"1998","journal-title":"Am J Hum Genet"},{"issue":"2","key":"2024012516213707600_bib48","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.cell.2018.02.047","article-title":"Common PIEZO1 allele in African populations causes\u00a0RBC dehydration and attenuates Plasmodium infection","volume":"173","author":"Ma","year":"2018","journal-title":"Cell"},{"key":"2024012516213707600_bib49","doi-asserted-by":"crossref","first-page":"1846","DOI":"10.1038\/s41467-019-09778-7","article-title":"An inner activation gate controls TMEM16F phospholipid scrambling","volume":"10","author":"Le","year":"2019","journal-title":"Nat Commun"},{"issue":"6","key":"2024012516213707600_bib52","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1038\/cdd.2016.7","article-title":"Exposure of phosphatidylserine on the cell surface","volume":"23","author":"Nagata","year":"2016","journal-title":"Cell Death Differ"},{"issue":"2","key":"2024012516213707600_bib51","doi-asserted-by":"crossref","first-page":"e202012704","DOI":"10.1085\/jgp.202012704","article-title":"Molecular underpinning of\u00a0intracellular pH regulation on TMEM16F","volume":"153","author":"Liang","year":"2021","journal-title":"J Gen Physiol"},{"issue":"6","key":"2024012516213707600_bib53","doi-asserted-by":"crossref","first-page":"C1553","DOI":"10.1152\/ajpcell.00186.2003","article-title":"Role of Ca2+-activated K+ channels in human erythrocyte apoptosis","volume":"285","author":"Lang","year":"2003","journal-title":"Am J Physiol Cell Physiol"},{"issue":"28","key":"2024012516213707600_bib54","doi-asserted-by":"crossref","first-page":"7804","DOI":"10.1073\/pnas.1606751113","article-title":"Biomechanics of red blood cells in human spleen and consequences for physiology and disease","volume":"113","author":"Pivkin","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6000","key":"2024012516213707600_bib55","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1126\/science.1193270","article-title":"Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels","volume":"330","author":"Coste","year":"2010","journal-title":"Science"},{"key":"2024012516213707600_bib56","doi-asserted-by":"crossref","first-page":"e07369","DOI":"10.7554\/eLife.07369","article-title":"Chemical activation of the mechanotransduction channel Piezo1","volume":"4","author":"Syeda","year":"2015","journal-title":"Elife"},{"issue":"12","key":"2024012516213707600_bib57","doi-asserted-by":"crossref","first-page":"E1162","DOI":"10.1073\/pnas.1219777110","article-title":"Xerocytosis is caused by mutations that alter the kinetics of the mechanosensitive channel PIEZO1","volume":"110","author":"Bae","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024012516213707600_bib58","doi-asserted-by":"crossref","first-page":"e82621","DOI":"10.7554\/eLife.82621","article-title":"Piezo1 as a force-through-membrane sensor in red blood cells","volume":"11","author":"Vaisey","year":"2022","journal-title":"Elife"},{"issue":"5","key":"2024012516213707600_bib59","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1085\/jgp.201210861","article-title":"TMEM16F (Anoctamin 6), an anion channel of delayed Ca2+ activation","volume":"141","author":"Grubb","year":"2013","journal-title":"J Gen Physiol"},{"key":"2024012516213707600_bib60","doi-asserted-by":"crossref","first-page":"e78840","DOI":"10.7554\/eLife.78840","article-title":"Functional coupling between TRPV4 channel and TMEM16F modulates human trophoblast fusion","volume":"11","author":"Zhang","year":"2022","journal-title":"Elife"},{"issue":"4","key":"2024012516213707600_bib61","doi-asserted-by":"crossref","first-page":"2348","DOI":"10.1016\/j.bbrc.2018.06.160","article-title":"TMEM16F\/ANO6, a Ca2+-activated anion channel, is negatively regulated by the actin cytoskeleton and intracellular MgATP","volume":"503","author":"Lin","year":"2018","journal-title":"Biochem\u00a0Biophys Res Commun"},{"issue":"11","key":"2024012516213707600_bib62","doi-asserted-by":"crossref","first-page":"4625","DOI":"10.1182\/blood-2001-12-0329","article-title":"Altered erythrocyte endothelial adherence and membrane phospholipid asymmetry in hereditary hydrocytosis","volume":"101","author":"Gallagher","year":"2003","journal-title":"Blood"},{"issue":"12","key":"2024012516213707600_bib63","doi-asserted-by":"crossref","first-page":"4529","DOI":"10.1074\/jbc.AC118.006530","article-title":"Drosophila Subdued is a moonlighting transmembrane protein 16 (TMEM16) that transports ions and phospholipids","volume":"294","author":"Le","year":"2019","journal-title":"J Biol Chem"},{"issue":"12","key":"2024012516213707600_bib64","doi-asserted-by":"crossref","first-page":"2681","DOI":"10.1182\/bloodadvances.2022008673","article-title":"Proteome alterations in erythrocytes with PIEZO1 gain-of-function mutations","volume":"7","author":"Andolfo","year":"2023","journal-title":"Blood Adv"},{"key":"2024012516213707600_bib65","doi-asserted-by":"crossref","first-page":"979","DOI":"10.3389\/fphys.2017.00979","article-title":"Red\u00a0blood cell passage of small capillaries is\u00a0associated with transient Ca2+-mediated adaptations","volume":"8","author":"Danielczok","year":"2017","journal-title":"Front Physiol"},{"issue":"29","key":"2024012516213707600_bib66","doi-asserted-by":"crossref","first-page":"6295","DOI":"10.1021\/bi200770q","article-title":"The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4","volume":"50","author":"Bae","year":"2011","journal-title":"Biochemistry"},{"issue":"40","key":"2024012516213707600_bib67","doi-asserted-by":"crossref","first-page":"16354","DOI":"10.1073\/pnas.1214596109","article-title":"Calcium-activated chloride channel TMEM16A modulates mucin secretion and airway smooth muscle contraction","volume":"109","author":"Huang","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"11","key":"2024012516213707600_bib68","doi-asserted-by":"crossref","first-page":"e163808","DOI":"10.1172\/JCI163808","article-title":"TMEM16E regulates endothelial cell procoagulant activity and thrombosis","volume":"133","author":"Schmaier","year":"2023","journal-title":"J Clin Invest"},{"issue":"5","key":"2024012516213707600_bib69","doi-asserted-by":"crossref","first-page":"625","DOI":"10.3390\/cancers11050625","article-title":"TMEM16F\/anoctamin 6 in ferroptotic cell death","volume":"11","author":"Ousingsawat","year":"2019","journal-title":"Cancers"},{"key":"2024012516213707600_bib70","doi-asserted-by":"crossref","first-page":"1142342","DOI":"10.3389\/fphar.2023.1142342","article-title":"Niclosamide does not modulate airway epithelial function through blocking of the calcium activated chloride channel, TMEM16A","volume":"14","author":"Danahay","year":"2023","journal-title":"Front Pharmacol"},{"issue":"2","key":"2024012516213707600_bib74","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1111\/jth.14360","article-title":"Red blood cells: the forgotten player in hemostasis and thrombosis","volume":"17","author":"Weisel","year":"2019","journal-title":"J Thromb Haemost"},{"key":"2024012516213707600_bib75","doi-asserted-by":"crossref","first-page":"629824","DOI":"10.3389\/fped.2021.629824","article-title":"Red blood cell contribution to hemostasis","volume":"9","author":"Gillespie","year":"2021","journal-title":"Front Pediatr"},{"issue":"3","key":"2024012516213707600_bib76","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1172\/JCI110297","article-title":"Exercise-induced hemolysis in xerocytosis. Erythrocyte dehydration and shear sensitivity","volume":"68","author":"Platt","year":"1981","journal-title":"J\u00a0Clin Invest"},{"issue":"1","key":"2024012516213707600_bib78","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1186\/s42358-019-0080-x","article-title":"Benzbromarone in the treatment of gout","volume":"59","author":"Azevedo","year":"2019","journal-title":"Adv Rheumatol"},{"issue":"8","key":"2024012516213707600_bib79","doi-asserted-by":"crossref","first-page":"643","DOI":"10.2165\/00002018-200831080-00002","article-title":"A\u00a0benefit-risk assessment of benzbromarone in the treatment of gout - was its withdrawal from the market in the best interest of patients?","volume":"31","author":"Lee","year":"2008","journal-title":"Drug Saf"},{"issue":"4","key":"2024012516213707600_bib80","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.cell.2021.01.024","article-title":"A\u00a0role of PIEZO1 in iron metabolism in mice and humans","volume":"184","author":"Ma","year":"2021","journal-title":"Cell"},{"issue":"7","key":"2024012516213707600_bib81","first-page":"4743","article-title":"Phosphatidylserine-exposed red blood cells and ineffective erythropoiesis biomarkers in patients with thalassemia","volume":"14","author":"Chansai","year":"2022","journal-title":"Am J Transl Res"},{"issue":"5","key":"2024012516213707600_bib82","doi-asserted-by":"crossref","first-page":"1873","DOI":"10.1182\/blood.V88.5.1873.1873","article-title":"Increased erythrocyte phosphatidylserine exposure in sickle cell disease: flow-cytometric measurement and clinical associations","volume":"88","author":"Wood","year":"1996","journal-title":"Blood"},{"issue":"22","key":"2024012516213707600_bib83","doi-asserted-by":"crossref","first-page":"9204","DOI":"10.1074\/jbc.M116.766196","article-title":"Evidence for shear-mediated Ca2+entry through mechanosensitive cation channels in human platelets and a megakaryocytic cell line","volume":"292","author":"Ilkan","year":"2017","journal-title":"J\u00a0Biol Chem"}],"container-title":["Blood"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/ashpublications.org\/blood\/article-pdf\/doi\/10.1182\/blood.2023021465\/2210313\/blood_bld-2023-021465-main.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/ashpublications.org\/blood\/article-pdf\/doi\/10.1182\/blood.2023021465\/2210313\/blood_bld-2023-021465-main.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,25]],"date-time":"2024-01-25T11:22:56Z","timestamp":1706181776000},"score":1,"resource":{"primary":{"URL":"https:\/\/ashpublications.org\/blood\/article\/143\/4\/357\/506380\/Deciphering-and-disrupting-PIEZO1-TMEM16F"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,1,25]]},"references-count":78,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2024,1,25]]}},"URL":"https:\/\/doi.org\/10.1182\/blood.2023021465","relation":{},"ISSN":["0006-4971","1528-0020"],"issn-type":[{"value":"0006-4971","type":"print"},{"value":"1528-0020","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,1,25]]}}}