{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T21:32:34Z","timestamp":1793223154448,"version":"4.5.0"},"reference-count":72,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T00:00:00Z","timestamp":1786060800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM127073"],"award-info":[{"award-number":["R35GM127073"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.jbc.2026.113432","type":"journal-article","created":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T23:37:25Z","timestamp":1786491445000},"page":"113432","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["The zinc metalloprotease ZMPSTE24 binds a distinct topological isoform of the tail-anchored protein IFITM3"],"prefix":"10.1016","volume":"302","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1980-0123","authenticated-orcid":false,"given":"Eric D.","family":"Spear","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-7422-862X","authenticated-orcid":false,"given":"Khurts","family":"Shilagardi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-5896-1517","authenticated-orcid":false,"given":"Sonia","family":"Sarju","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5851-5021","authenticated-orcid":false,"given":"Susan","family":"Michaelis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113432_bib1","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1002\/pro.3074","article-title":"Human CaaX protease ZMPSTE24 expressed in yeast: structure and inhibition by HIV protease inhibitors","volume":"26","author":"Clark","year":"2017","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2026.113432_bib2","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1126\/science.1232048","article-title":"Structure of the integral membrane protein CAAX protease Ste24p","volume":"339","author":"Pryor","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib3","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1126\/science.1231513","article-title":"The structural basis of ZMPSTE24-dependent laminopathies","volume":"339","author":"Quigley","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib4","series-title":"Handbook of Proteolytic Enzymes: Metallopeptidases,4th Ed","first-page":"537","article-title":"Mammalian zinc metalloprotease ZMPSTE24 and yeast Ste24","author":"Spear","year":"2025"},{"key":"10.1016\/j.jbc.2026.113432_bib5","doi-asserted-by":"crossref","first-page":"13049","DOI":"10.1073\/pnas.192460799","article-title":"Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect","volume":"99","author":"Bergo","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113432_bib6","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1186\/gb-2011-12-5-222","article-title":"The lamin protein family","volume":"12","author":"Dittmer","year":"2011","journal-title":"Genome Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib7","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/ng871","article-title":"Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice","volume":"31","author":"Pendas","year":"2002","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jbc.2026.113432_bib8","doi-asserted-by":"crossref","first-page":"1796","DOI":"10.1126\/science.275.5307.1796","article-title":"Modulation of Ras and a-factor function by carboxyl-terminal proteolysis","volume":"275","author":"Boyartchuk","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib9","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1093\/genetics\/150.1.95","article-title":"Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor","volume":"150","author":"Boyartchuk","year":"1998","journal-title":"Genetics"},{"key":"10.1016\/j.jbc.2026.113432_bib10","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1083\/jcb.136.2.271","article-title":"A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor","volume":"136","author":"Fujimura-Kamada","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib11","doi-asserted-by":"crossref","first-page":"6227","DOI":"10.1074\/jbc.275.9.6227","article-title":"Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis","volume":"275","author":"Schmidt","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib12","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1083\/jcb.142.3.635","article-title":"Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing","volume":"142","author":"Tam","year":"1998","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib13","doi-asserted-by":"crossref","first-page":"46798","DOI":"10.1074\/jbc.M106150200","article-title":"The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor","volume":"276","author":"Tam","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib14","doi-asserted-by":"crossref","first-page":"4084","DOI":"10.1093\/hmg\/dds233","article-title":"Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severity","volume":"21","author":"Barrowman","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2026.113432_bib15","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.ymeth.2019.01.001","article-title":"A humanized yeast system to analyze cleavage of prelamin A by ZMPSTE24","volume":"157","author":"Spear","year":"2019","journal-title":"Methods"},{"key":"10.1016\/j.jbc.2026.113432_bib16","doi-asserted-by":"crossref","DOI":"10.1242\/dmm.033670","article-title":"ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and\/or protein stability","volume":"11","author":"Spear","year":"2018","journal-title":"Dis. Model. Mech."},{"key":"10.1016\/j.jbc.2026.113432_bib17","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1126\/science.1180823","article-title":"The genetic landscape of a cell","volume":"327","author":"Costanzo","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib18","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1534\/g3.117.040220","article-title":"TheCellMap.org: a web-accessible database for visualizing and mining the global yeast genetic interaction network","volume":"7","author":"Usaj","year":"2017","journal-title":"G3 (Bethesda)"},{"key":"10.1016\/j.jbc.2026.113432_bib19","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1091\/mbc.01-10-0488","article-title":"Yeast genes controlling responses to topogenic signals in a model transmembrane protein","volume":"13","author":"Tipper","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2026.113432_bib20","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1126\/science.1167983","article-title":"Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum","volume":"323","author":"Jonikas","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib21","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.cell.2015.11.053","article-title":"The protease Ste24 clears clogged translocons","volume":"164","author":"Ast","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113432_bib22","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1084\/jem.20161270","article-title":"ZMPSTE24 defends against influenza and other pathogenic viruses","volume":"214","author":"Fu","year":"2017","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jbc.2026.113432_bib23","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1089\/dna.2017.3791","article-title":"ZMPSTE24 is downstream effector of interferon-induced transmembrane antiviral activity","volume":"36","author":"Li","year":"2017","journal-title":"DNA Cell Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib24","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.02543-22","article-title":"The integral membrane protein ZMPSTE24 protects cells from SARS-CoV-2 spike-mediated pseudovirus infection and syncytia formation","volume":"13","author":"Shilagardi","year":"2022","journal-title":"mBio"},{"key":"10.1016\/j.jbc.2026.113432_bib25","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2022.840885","article-title":"Inhibition of arenavirus entry and replication by the cell-intrinsic restriction factor ZMPSTE24 is enhanced by IFITM antiviral activity","volume":"13","author":"Stott-Marshall","year":"2022","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2026.113432_bib26","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/j.cell.2009.12.017","article-title":"The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, west Nile virus, and Dengue virus","volume":"139","author":"Brass","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113432_bib27","doi-asserted-by":"crossref","first-page":"1740","DOI":"10.15252\/embr.201744100","article-title":"IFITM3 requires an amphipathic helix for antiviral activity","volume":"18","author":"Chesarino","year":"2017","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jbc.2026.113432_bib28","doi-asserted-by":"crossref","first-page":"7837","DOI":"10.1128\/JVI.00481-13","article-title":"The CD225 domain of IFITM3 is required for both IFITM protein association and inhibition of influenza A virus and dengue virus replication","volume":"87","author":"John","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.113432_bib29","first-page":"1582","article-title":"IFITM3 restricts human metapneumovirus","volume":"218","author":"McMichael","year":"2018","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jbc.2026.113432_bib30","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020106501","article-title":"Opposing activities of IFITM proteins in SARS-CoV-2 infection","volume":"40","author":"Shi","year":"2021","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113432_bib31","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01535-17","article-title":"Identification of residues controlling restriction versus enhancing activities of IFITM proteins on entry of human Coronaviruses","volume":"92","author":"Zhao","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.113432_bib32","doi-asserted-by":"crossref","first-page":"4584","DOI":"10.1038\/s41467-021-24817-y","article-title":"IFITM proteins promote SARS-CoV-2 infection and are targets for virus inhibition in vitro","volume":"12","author":"Prelli Bozzo","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113432_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2023.106395","article-title":"Endogenous IFITMs boost SARS-coronavirus 1 and 2 replication whereas overexpression inhibits infection by relocalizing ACE2","volume":"26","author":"Xie","year":"2023","journal-title":"iScience"},{"key":"10.1016\/j.jbc.2026.113432_bib34","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1186\/s12977-017-0377-y","article-title":"More than meets the I: the diverse antiviral and cellular functions of interferon-induced transmembrane proteins","volume":"14","author":"Shi","year":"2017","journal-title":"Retrovirology"},{"key":"10.1016\/j.jbc.2026.113432_bib35","doi-asserted-by":"crossref","first-page":"32184","DOI":"10.1074\/jbc.M113.514356","article-title":"Interferon-induced transmembrane protein 3 is a type II transmembrane protein","volume":"288","author":"Bailey","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib36","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0104341","article-title":"A membrane topology model for human interferon inducible transmembrane protein 1","volume":"9","author":"Weston","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113432_bib37","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004048","article-title":"IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion","volume":"10","author":"Desai","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.113432_bib38","doi-asserted-by":"crossref","first-page":"8155","DOI":"10.1021\/acsnano.0c10567","article-title":"Interferon-induced transmembrane protein 3 blocks fusion of diverse enveloped viruses by altering mechanical properties of cell membranes","volume":"15","author":"Guo","year":"2021","journal-title":"ACS Nano"},{"key":"10.1016\/j.jbc.2026.113432_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003124","article-title":"IFITM proteins restrict viral membrane hemifusion","volume":"9","author":"Li","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.113432_bib40","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2022.167759","article-title":"Cholesterol binds the amphipathic helix of IFITM3 and regulates antiviral activity","volume":"434","author":"Rahman","year":"2022","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib41","doi-asserted-by":"crossref","first-page":"9923","DOI":"10.1128\/JVI.00621-13","article-title":"Palmitoylation on conserved and nonconserved cysteines of murine IFITM1 regulates its stability and anti-influenza a virus activity","volume":"87","author":"Hach","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.jbc.2026.113432_bib42","doi-asserted-by":"crossref","first-page":"4302","DOI":"10.1073\/pnas.1602244113","article-title":"Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation","volume":"113","author":"Percher","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113432_bib43","doi-asserted-by":"crossref","first-page":"19631","DOI":"10.1074\/jbc.M112.362095","article-title":"S-palmitoylation and ubiquitination differentially regulate interferon-induced transmembrane protein 3 (IFITM3)-mediated resistance to influenza virus","volume":"287","author":"Yount","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib44","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nchembio.405","article-title":"Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3","volume":"6","author":"Yount","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib45","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.58537","article-title":"Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state","volume":"9","author":"Rahman","year":"2020","journal-title":"Elife"},{"issue":"7","key":"10.1016\/j.jbc.2026.113432_bib46","doi-asserted-by":"crossref","first-page":"e0067726","DOI":"10.1128\/jvi.00677-26","article-title":"IFITM1 and IFITM3 cooperate to restrict virus entry in endolysosomes","volume":"100","author":"Wilt","year":"2026","journal-title":"J Virol"},{"key":"10.1016\/j.jbc.2026.113432_bib47","doi-asserted-by":"crossref","first-page":"3859","DOI":"10.3390\/ijms20163859","article-title":"Analysis of IFITM-IFITM interactions by a flow cytometry-based FRET assay","volume":"20","author":"Winkler","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113432_bib48","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1007\/s007750100295","article-title":"A theoretical study of the mechanism for peptide hydrolysis by thermolysin","volume":"7","author":"Pelmenschikov","year":"2002","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101272","article-title":"A bioorthogonal chemical reporter for fatty acid synthase-dependent protein acylation","volume":"297","author":"Karthigeyan","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib50","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.11306","article-title":"ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras palmitate turnover and subcellular localization","volume":"4","author":"Lin","year":"2015","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2026.113432_bib51","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/0003-2697(85)90390-2","article-title":"The reaction of horseradish peroxidase with hydroperoxides derived from Triton X-100","volume":"146","author":"Miki","year":"1985","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2026.113432_bib52","doi-asserted-by":"crossref","first-page":"4277","DOI":"10.1016\/j.molcel.2022.09.035","article-title":"ATP13A1 prevents ERAD of folding-competent mislocalized and misoriented proteins","volume":"82","author":"McKenna","year":"2022","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113432_bib53","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a041252","article-title":"A TAle of two pathways: tail-anchored protein insertion at the endoplasmic reticulum","volume":"15","author":"Guna","year":"2023","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib54","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1038\/s41594-024-01296-5","article-title":"A unifying model for membrane protein biogenesis","volume":"31","author":"Hegde","year":"2024","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib55","doi-asserted-by":"crossref","first-page":"1917","DOI":"10.1016\/j.molcel.2024.04.010","article-title":"An ATP13A1-assisted topogenesis pathway for folding multi-spanning membrane proteins","volume":"84","author":"Ji","year":"2024","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113432_bib56","doi-asserted-by":"crossref","first-page":"8777","DOI":"10.1038\/s41467-024-53097-5","article-title":"Secretion of endoplasmic reticulum protein VAPB\/ALS8 requires topological inversion","volume":"15","author":"Kamemura","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113432_bib57","article-title":"Topological regulation of a transmembrane protein by luminal-to-cytosolic retrotranslocation of glycosylated sequence","volume":"42","author":"Wang","year":"2023","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113432_bib58","first-page":"898","article-title":"Transmembrane dislocases: a second chance for protein targeting trends","volume":"31","author":"Dederer","year":"2021","journal-title":"Cell Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib59","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a041249","article-title":"The endoplasmic reticulum and the fidelity of nascent protein localization","volume":"15","author":"McKenna","year":"2023","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib60","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2023.1220441","article-title":"Spf1 and Ste24: quality controllers of transmembrane protein topology in the eukaryotic cell","volume":"11","author":"Tipper","year":"2023","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib61","doi-asserted-by":"crossref","DOI":"10.1126\/science.abc5809","article-title":"The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase","volume":"369","author":"McKenna","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib62","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.230094","article-title":"A trap mutant reveals the physiological client spectrum of TRC40","volume":"132","author":"Coy-Vergara","year":"2019","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113432_bib63","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1111\/mmi.12241","article-title":"Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development","volume":"88","author":"Bhat","year":"2013","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.113432_bib64","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/S1097-2765(03)00060-1","article-title":"Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals","volume":"11","author":"Flynn","year":"2003","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113432_bib65","doi-asserted-by":"crossref","first-page":"42962","DOI":"10.1074\/jbc.M112.388470","article-title":"A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli","volume":"287","author":"Westphal","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113432_bib66","doi-asserted-by":"crossref","DOI":"10.1126\/science.abi6983","article-title":"OpenCell: endogenous tagging for the cartography of human cellular Organization","volume":"375","author":"Cho","year":"2022","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113432_bib67","doi-asserted-by":"crossref","first-page":"5991","DOI":"10.1038\/s41467-021-26225-8","article-title":"PGRMC1 acts as a size-selective cargo receptor to drive ER-phagic clearance of mutant prohormones","volume":"12","author":"Chen","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113432_bib68","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/s41598-018-37441-6","article-title":"Epitope mapping of anti-PGRMC1 antibodies reveals the non-conventional membrane topology of PGRMC1 on the cell surface","volume":"9","author":"Kim","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113432_bib69","doi-asserted-by":"crossref","DOI":"10.1016\/j.pharmthera.2022.108326","article-title":"PGRMC1: an enigmatic heme-binding protein","volume":"241","author":"McGuire","year":"2023","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.jbc.2026.113432_bib70","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2022.102467","article-title":"Interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity","volume":"77","author":"Jimenez-Munguia","year":"2022","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113432_bib71","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.3390\/v16101543","article-title":"Research progress into the biological functions of IFITM3","volume":"16","author":"Xie","year":"2024","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2026.113432_bib72","doi-asserted-by":"crossref","first-page":"E4671","DOI":"10.1073\/pnas.1602419113","article-title":"AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrity","volume":"113","author":"Di Micco","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826023045?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826023045?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T20:39:28Z","timestamp":1793219968000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826023045"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":72,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026,10]]}},"alternative-id":["S0021925826023045"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113432","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The zinc metalloprotease ZMPSTE24 binds a distinct topological isoform of the tail-anchored protein IFITM3","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113432","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113432"}}