{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T22:41:59Z","timestamp":1787611319473,"version":"build-2736575974"},"reference-count":21,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2024,12,10]],"date-time":"2024-12-10T00:00:00Z","timestamp":1733788800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/\u00a0","name":"KAKENHI","doi-asserted-by":"publisher","award":["JP22K06155"],"award-info":[{"award-number":["JP22K06155"]}],"id":[{"id":"10.13039\/\u00a0","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,2,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Glycosylphosphatidylinositol (GPI) anchoring is a conserved post-translational modification in eukaryotes. This modification allows acceptor proteins to be expressed at the cell surface as GPI-anchored proteins (GPI-APs), which play critical roles in various biological processes. It has been proposed that remodelling of GPI after transferring acceptor proteins, including the PGAP1-dependent deacylation of GPI-inositol, functions as a checkpoint for transporting mature GPI-APs from the endoplasmic reticulum (ER) to the Golgi. A previous study identified several factors involved in regulating PGAP1-dependent GPI-inositol deacylation, including proteins associated with the calnexin cycles, SELT and CLPTM1. A recent report by Cao et\u00a0al., revealed that the loss of TMEM41B, an ER-resident lipid scramblase, rescues the defect in GPI-inositol deacylation in SELT-KO cells. Further investigation demonstrated that TMEM41B is essential for the efficient transport of both GPI-APs and transmembrane proteins from the ER to the Golgi. The study also found that PGAP1 proteins accumulate in the ER of TMEM41B-KO cells, suggesting that perturbations in the ER-membrane lipid integrity stabilize PGAP1 proteins, thereby enhancing the PGAP1 activity within the ER. These findings highlight that defects in TMEM41B impact two distinct processes: (i) the transport of GPI-APs from the ER to the Golgi, and (ii) the deacylation of GPI-APs.<\/jats:p>","DOI":"10.1093\/jb\/mvae085","type":"journal-article","created":{"date-parts":[[2024,12,11]],"date-time":"2024-12-11T02:01:01Z","timestamp":1733882461000},"page":"69-71","source":"Crossref","is-referenced-by-count":2,"title":["Commentary for: a lipid scramblase TMEM41B is involved in the processing and transport of GPI-anchored proteins"],"prefix":"10.1093","volume":"177","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1909-9488","authenticated-orcid":false,"given":"Hiroto","family":"Hirayama","sequence":"first","affiliation":[{"name":"Glycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research (CPR), RIKEN , 2-1 Hirosawa, Wako, Saitama 351-0198 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,12,10]]},"reference":[{"key":"2025020512014254700_ref1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/glycob\/cww086","article-title":"Biological roles of glycans","volume":"27","author":"Varki","year":"2017","journal-title":"Glycobiology"},{"key":"2025020512014254700_ref2","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.190290","article-title":"Biosynthesis and biology of mammalian GPI-anchored proteins","volume":"10","author":"Kinoshita","year":"2020","journal-title":"Open Biol."},{"key":"2025020512014254700_ref3","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1042\/BST20191142","article-title":"Mammalian GPI-anchor modifications and the enzymes involved","volume":"48","author":"Liu","year":"2020","journal-title":"Biochem. 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USA"},{"key":"2025020512014254700_ref9","doi-asserted-by":"crossref","first-page":"4285","DOI":"10.1091\/mbc.e03-03-0193","article-title":"PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor","volume":"14","author":"Murakami","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"2025020512014254700_ref10","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1080\/09687860600601494","article-title":"Recent developments in the molecular, biochemical and functional characterization of GPI8 and the GPI-anchoring mechanism [review]","volume":"23","author":"Zacks","year":"2006","journal-title":"Mol. Membr. Biol."},{"key":"2025020512014254700_ref11","doi-asserted-by":"crossref","first-page":"12168","DOI":"10.1016\/S0021-9258(19)49819-0","article-title":"Phosphatidylinositol glycan (PI-G) anchored membrane proteins. Amino acid requirements adjacent to the site of cleavage and PI-G attachment in the COOH-terminal signal peptide","volume":"267","author":"Gerber","year":"1992","journal-title":"J. Biol. Chem."},{"key":"2025020512014254700_ref12","doi-asserted-by":"crossref","first-page":"14256","DOI":"10.1074\/jbc.M313755200","article-title":"Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p","volume":"279","author":"Tanaka","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2025020512014254700_ref13","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.cell.2009.08.040","article-title":"GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi","volume":"139","author":"Fujita","year":"2009","journal-title":"Cell"},{"key":"2025020512014254700_ref14","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1083\/jcb.201012074","article-title":"Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI","volume":"194","author":"Fujita","year":"2011","journal-title":"J. Cell Biol."},{"key":"2025020512014254700_ref15","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1083\/jcb.201706135","article-title":"N-glycan-dependent protein folding and endoplasmic reticulum retention regulate GPI-anchor processing","volume":"217","author":"Liu","year":"2018","journal-title":"J. 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