{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T01:30:36Z","timestamp":1791509436569,"version":"4.3.4"},"reference-count":168,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T00:00:00Z","timestamp":1784160000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100011033","name":"Agencia Estatal de Investigaci\u00f3n","doi-asserted-by":"crossref","award":["AEI\/10.13039\/501100011033\/PID2022-136665NB-I00"],"award-info":[{"award-number":["AEI\/10.13039\/501100011033\/PID2022-136665NB-I00"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"crossref"}]},{"award":["AEI\/10.13039\/501100011033\/PID2022-136665NB-I00"],"award-info":[{"award-number":["AEI\/10.13039\/501100011033\/PID2022-136665NB-I00"]}],"id":[{"id":"https:\/\/ror.org\/003x0zc53","id-type":"ROR","asserted-by":"publisher"}]},{"name":"National Institute of General Medical Sciences, National Institutes of Health","award":["R01 GM134327"],"award-info":[{"award-number":["R01 GM134327"]}]},{"award":["R01 GM134327"],"award-info":[{"award-number":["R01 GM134327"]}],"id":[{"id":"https:\/\/ror.org\/04q48ey07","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are a distinct class of eukaryotic cell-surface proteins characterized by a glycolipid anchor at their C-terminus. They display unique biophysical properties and play important roles in human diseases, including transmissible spongiform encephalopathies (TSEs), malaria, sleeping sickness, and rare disorders collectively termed inherited GPI deficiency (IGD). Because of their broad clinical relevance, GPI-APs have become a major focus of research, including their intracellular quality control (QC). Studies in diverse model organisms have revealed striking interspecies differences in GPI-AP QC pathways and notable distinctions from QC mechanisms and the degradation of misfolded species governing other secretory proteins. In this review, we summarize recent advances in the understanding of these cellular processes and propose that the observed variations in QC reflect distinct cellular strategies that balance protein QC with membrane homeostasis across evolutionary contexts.<\/jats:p>","DOI":"10.3390\/ijms27146316","type":"journal-article","created":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T06:49:36Z","timestamp":1784184576000},"page":"6316","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Mechanisms of Quality Control in GPI-Anchored Proteins: The Central Role of the Lipid Anchor"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6723-1290","authenticated-orcid":false,"given":"Leticia","family":"Lemus","sequence":"first","affiliation":[{"name":"Department of Genetics, University of Seville, Av. Reina Mercedes, 6, 41012 Seville, Spain"},{"name":"Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1210-4021","authenticated-orcid":false,"given":"Prasanna","family":"Satpute-Krishnan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0854-4873","authenticated-orcid":false,"given":"Veit","family":"Goder","sequence":"additional","affiliation":[{"name":"Department of Genetics, University of Seville, Av. Reina Mercedes, 6, 41012 Seville, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0304-4157(97)00005-1","article-title":"Mammalian GPI Proteins: Sorting, Membrane Residence and Functions","volume":"1331","author":"Nosjean","year":"1997","journal-title":"Biochim. Biophys. Acta (BBA)-Rev. Biomembr."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1194\/jlr.R700002-JLR200","article-title":"Thematic Review Series: Lipid Posttranslational Modifications. GPI Anchoring of Protein in Yeast and Mammalian Cells, or: How We Learned to Stop Worrying and Love Glycophospholipids","volume":"48","author":"Orlean","year":"2007","journal-title":"J. Lipid Res."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"190290","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":"ref_4","doi-asserted-by":"crossref","first-page":"cwae061","DOI":"10.1093\/glycob\/cwae061","article-title":"Towards a Thorough Understanding of Mammalian Glycosylphosphatidylinositol-Anchored Protein Biosynthesis","volume":"34","author":"Kinoshita","year":"2024","journal-title":"Glycobiology"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1093\/emboj\/17.4.877","article-title":"The First Step of Glycosylphosphatidylinositol Biosynthesis Is Mediated by a Complex of PIG-A, PIG-H, PIG-C and GPI1","volume":"17","author":"Watanabe","year":"1998","journal-title":"EMBO J."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"4402","DOI":"10.1093\/emboj\/19.16.4402","article-title":"Initial Enzyme for Glycosylphosphatidylinositol Biosynthesis Requires PIG-P and Is Regulated by DPM2","volume":"19","author":"Watanabe","year":"2000","journal-title":"EMBO J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1042\/bj3390185","article-title":"Mammalian PIG-L and Its Yeast Homologue Gpi12p Are N-Acetylglucosaminylphosphatidylinositol de-N-Acetylases Essential in Glycosylphosphatidylinositol Biosynthesis","volume":"339","author":"Watanabe","year":"1999","journal-title":"Biochem. J."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"e2115083119","DOI":"10.1073\/pnas.2115083119","article-title":"Genome-Wide CRISPR Screen Reveals CLPTM1L as a Lipid Scramblase Required for Efficient Glycosylphosphatidylinositol Biosynthesis","volume":"119","author":"Wang","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","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":"ref_10","doi-asserted-by":"crossref","first-page":"2378","DOI":"10.1002\/1873-3468.13465","article-title":"On the Road to Unraveling the Molecular Functions of Ether Lipids","volume":"593","author":"Riezman","year":"2019","journal-title":"FEBS Lett."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4254","DOI":"10.1002\/j.1460-2075.1996.tb00800.x","article-title":"PIG-B, a Membrane Protein of the Endoplasmic Reticulum with a Large Lumenal Domain, Is Involved in Transferring the Third Mannose of the GPI Anchor","volume":"15","author":"Takahashi","year":"1996","journal-title":"EMBO J."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"9489","DOI":"10.1074\/jbc.M413867200","article-title":"PIG-V Involved in Transferring the Second Mannose in Glycosylphosphatidylinositol","volume":"280","author":"Ji","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1093\/emboj\/20.1.250","article-title":"PIG-M Transfers the First Mannose to Glycosylphosphatidylinositol on the Lumenal Side of the ER","volume":"20","author":"Maeda","year":"2001","journal-title":"EMBO J."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"20911","DOI":"10.1074\/jbc.M001913200","article-title":"Requirement of PIG-F and PIG-O for Transferring Phosphoethanolamine to the Third Mannose in Glycosylphosphatidylinositol","volume":"275","author":"Hong","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1907","DOI":"10.1002\/j.1460-2075.1993.tb05839.x","article-title":"Phosphatidylethanolamine Is the Donor of the Terminal Phosphoethanolamine Group in Trypanosome Glycosylphosphatidylinositols","volume":"12","author":"Menon","year":"1993","journal-title":"EMBO J."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"9728","DOI":"10.1074\/jbc.M413755200","article-title":"GPI7 Is the Second Partner of PIG-F and Involved in Modification of Glycosylphosphatidylinositol","volume":"280","author":"Shishioh","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"35099","DOI":"10.1074\/jbc.274.49.35099","article-title":"Pig-n, a Mammalian Homologue of Yeast Mcd4p, Is Involved in Transferring Phosphoethanolamine to the First Mannose of the Glycosylphosphatidylinositol","volume":"274","author":"Hong","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1083\/jcb.114.1.61","article-title":"Transfer of Glycosyl-Phosphatidylinositol Membrane Anchors to Polypeptide Acceptors in a Cell-Free System","volume":"114","author":"Mayor","year":"1991","journal-title":"J. Cell Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"19576","DOI":"10.1074\/jbc.270.33.19576","article-title":"An Active Carbonyl Formed during Glycosylphosphatidylinositol Addition to a Protein Is Evidence of Catalysis by a Transamidase","volume":"270","author":"Maxwell","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"16479","DOI":"10.1074\/jbc.274.23.16479","article-title":"A Cell-Free Assay for Glycosylphosphatidylinositol Anchoring in African Trypanosomes. Demonstration of a Transamidation Reaction Mechanism","volume":"274","author":"Sharma","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5520","DOI":"10.1038\/s41467-023-41281-y","article-title":"Structures of Liganded Glycosylphosphatidylinositol Transamidase Illuminate GPI-AP Biogenesis","volume":"14","author":"Xu","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1007\/978-3-031-58843-3_16","article-title":"Structure and Function of the Glycosylphosphatidylinositol Transamidase, a Transmembrane Complex Catalyzing GPI Anchoring of Proteins","volume":"Volume 104","author":"Li","year":"2024","journal-title":"Macromolecular Protein Complexes V"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"27731","DOI":"10.1074\/jbc.M101986200","article-title":"The Essential Smp3 Protein Is Required for Addition of the Side-Branching Fourth Mannose during Assembly of Yeast Glycosylphosphatidylinositols","volume":"276","author":"Grimme","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5043","DOI":"10.1021\/bi00136a600","article-title":"Glycosylinositol Phospholipid Anchors of the Scrapie and Cellular Prion Proteins Contain Sialic Acid","volume":"31","author":"Stahl","year":"1992","journal-title":"Biochemistry"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"EMBR202154352","DOI":"10.15252\/embr.202154352","article-title":"Ethanolamine-phosphate on the Second Mannose Is a Preferential Bridge for Some GPI-anchored Proteins","volume":"23","author":"Ishida","year":"2022","journal-title":"EMBO Rep."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/0092-8674(92)90189-J","article-title":"Sorting of GPI-Anchored Proteins to Glycolipid-Enriched Membrane Subdomains during Transport to the Apical Cell Surface","volume":"68","author":"Brown","year":"1992","journal-title":"Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1194\/jlr.R062760","article-title":"Trafficking of Glycosylphosphatidylinositol Anchored Proteins from the Endoplasmic Reticulum to the Cell Surface","volume":"57","author":"Muniz","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1126\/science.3276003","article-title":"Structural and Functional Roles of Glycosyl-Phosphatidylinositol in Membranes","volume":"239","author":"Low","year":"1988","journal-title":"Science"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1080\/13813455.2018.1498904","article-title":"Membrane Insertion and Intercellular Transfer of Glycosylphosphatidylinositol-Anchored Proteins: Potential Therapeutic Applications","volume":"126","year":"2020","journal-title":"Arch. Physiol. Biochem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nchembio834","article-title":"Trafficking and Signaling by Fatty-Acylated and Prenylated Proteins","volume":"2","author":"Resh","year":"2006","journal-title":"Nat. Chem. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/nrm2084","article-title":"Palmitoylation: Policing Protein Stability and Traffic","volume":"8","author":"Linder","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"6991","DOI":"10.1021\/bi8006324","article-title":"The Glycosylphosphatidylinositol Anchor: A Complex Membrane-Anchoring Structure for Proteins","volume":"47","author":"Paulick","year":"2008","journal-title":"Biochemistry"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/35036052","article-title":"Lipid Rafts and Signal Transduction","volume":"1","author":"Simons","year":"2000","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1111\/j.1600-0854.2004.0181.x","article-title":"Lipids as Targeting Signals: Lipid Rafts and Intracellular Trafficking","volume":"5","author":"Helms","year":"2004","journal-title":"Traffic"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1002\/1873-3468.14830","article-title":"Protein Sorting upon Exit from the Endoplasmic Reticulum Dominates Golgi Biogenesis in Budding Yeast","volume":"598","author":"Sasaki","year":"2024","journal-title":"FEBS Lett."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"7479","DOI":"10.1073\/pnas.96.13.7479","article-title":"X Inactivation and Somatic Cell Selection Rescue Female Mice Carrying a Piga-Null Mutation","volume":"96","author":"Keller","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7938","DOI":"10.1073\/pnas.93.15.7938","article-title":"A Knock-out Model of Paroxysmal Nocturnal Hemoglobinuria: Pig-a(-) Hematopoiesis Is Reconstituted Following Intercellular Transfer of GPI-Anchored Proteins","volume":"93","author":"Dunn","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"10193","DOI":"10.1016\/S0021-9258(17)34042-5","article-title":"A Conditionally Lethal Yeast Mutant Blocked at the First Step in Glycosyl Phosphatidylinositol Anchor Synthesis","volume":"269","author":"Leidich","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.1091\/mbc.e02-03-0167","article-title":"Essential Roles for GPI-Anchored Proteins in African Trypanosomes Revealed Using Mutants Deficient in GPI8","volume":"14","author":"Lillico","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"22061","DOI":"10.1073\/pnas.2010661117","article-title":"Structural Base for the Transfer of GPI-Anchored Glycoproteins into Fungal Cell Walls","volume":"117","author":"Vogt","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1017\/S0031182009992034","article-title":"Bloodstream Form Trypanosome Plasma Membrane Proteins: Antigenic Variation and Invariant Antigens","volume":"137","author":"Schwede","year":"2010","journal-title":"Parasitology"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1126\/science.2443973","article-title":"A Glycan-Phosphatidylinositol-Specific Phospholipase D in Human Serum","volume":"238","author":"Davitz","year":"1987","journal-title":"Science"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/nm1179","article-title":"Angiotensin-Converting Enzyme Is a GPI-Anchored Protein Releasing Factor Crucial for Fertilization","volume":"11","author":"Kondoh","year":"2005","journal-title":"Nat. Med."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"31643","DOI":"10.1074\/jbc.M702713200","article-title":"Growth Factor Induction of Cripto-1 Shedding by Glycosylphosphatidylinositol-Phospholipase D and Enhancement of Endothelial Cell Migration","volume":"282","author":"Watanabe","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1111\/febs.12699","article-title":"The Emerging Physiological Roles of the Glycerophosphodiesterase Family","volume":"281","author":"Corda","year":"2014","journal-title":"FEBS J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1194\/jlr.R063032","article-title":"GPI-AP Release in Cellular, Developmental, and Reproductive Biology","volume":"57","author":"Fujihara","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/370295a0","article-title":"Prion Protein Is Necessary for Normal Synaptic Function","volume":"370","author":"Collinge","year":"1994","journal-title":"Nature"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"e12941","DOI":"10.1111\/bpa.12941","article-title":"Accumulation of Cellular Prion Protein within \u03b2-Amyloid Oligomer Plaques in Aged Human Brains","volume":"31","author":"Takahashi","year":"2021","journal-title":"Brain Pathol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1093\/brain\/awt375","article-title":"High Molecular Mass Assemblies of Amyloid-\u03b2 Oligomers Bind Prion Protein in Patients with Alzheimer\u2019s Disease","volume":"137","author":"Dohler","year":"2014","journal-title":"Brain"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"6776","DOI":"10.1002\/alz.14120","article-title":"Cellular Prion Protein Acts as Mediator of Amyloid Beta Uptake by Caveolin-1 Causing Cellular Dysfunctions In Vitro and In Vivo","volume":"20","author":"Schmitz","year":"2024","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/ncomms1341","article-title":"Interaction between Prion Protein and Toxic Amyloid \u03b2 Assemblies Can Be Therapeutically Targeted at Multiple Sites","volume":"2","author":"Freir","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"28625","DOI":"10.1073\/pnas.2009238117","article-title":"Evidence for Aggregation-Independent, PrPC-Mediated A\u03b2 Cellular Internalization","volume":"117","author":"Foley","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1038\/nature07761","article-title":"Cellular Prion Protein Mediates Impairment of Synaptic Plasticity by Amyloid-Beta Oligomers","volume":"457","author":"Gimbel","year":"2009","journal-title":"Nature"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1080\/19336896.2017.1423186","article-title":"The Role of the Prion Protein in the Internalization of \u03b1-Synuclein Amyloids","volume":"12","author":"Legname","year":"2018","journal-title":"Prion"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1007\/s12035-017-0451-4","article-title":"Involvement of Cellular Prion Protein in \u03b1-Synuclein Transport in Neurons","volume":"55","author":"Urrea","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"ref_56","first-page":"55","article-title":"Molecular Biology of Prions Causing Infectious and Genetic Encephalopathies of Humans as Well as Scrapie of Sheep and BSE of Cattle","volume":"75","author":"Prusiner","year":"1991","journal-title":"Dev. Biol. Stand."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1007\/s00109-022-02245-9","article-title":"The Multiple Functions of PrPC in Physiological, Cancer, and Neurodegenerative Contexts","volume":"100","author":"Grimaldi","year":"2022","journal-title":"J. Mol. Med."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Dvorakova, E., Vranac, T., Janouskova, O., \u010cernilec, M., Koren, S., Lukan, A., Nov\u00e1kov\u00e1, J., Matej, R., Holada, K., and \u0160erbec, V.T. (2013). Detection of the GPI-Anchorless Prion Protein Fragment PrP226* in Human Brain. BMC Neurol., 13.","DOI":"10.1186\/1471-2377-13-126"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"4870","DOI":"10.1074\/jbc.M113.531335","article-title":"Gerstmann-Str\u00e4ussler-Scheinker Disease and Anchorless Prion Protein Mice Share Prion Conformational Properties Diverging from Sporadic Creutzfeldt-Jakob Disease","volume":"289","author":"Zanusso","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s12035-020-02098-8","article-title":"Characterization of Anchorless Human PrP with Q227X Stop Mutation Linked to Gerstmann-Str\u00e4ussler-Scheinker Syndrome In Vivo and In Vitro","volume":"58","author":"Shen","year":"2021","journal-title":"Mol. Neurobiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.3724\/abbs.2024128","article-title":"Inherited Glycosylphosphatidylinositol Deficiency: A Review from Molecular and Clinical Perspectives","volume":"56","author":"Li","year":"2024","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.ajhg.2019.05.019","article-title":"Mutations in PIGB Cause an Inherited GPI Biosynthesis Defect with an Axonal Neuropathy and Metabolic Abnormality in Severe Cases","volume":"105","author":"Murakami","year":"2019","journal-title":"Am. J. Hum. Genet."},{"key":"ref_63","first-page":"5","article-title":"Inherited GPI Deficiencies: A New Disease with Intellectual Disability and Epilepsy","volume":"47","author":"Murakami","year":"2015","journal-title":"No To Hattatsu"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1111\/cge.13425","article-title":"Clinical Variability in Inherited Glycosylphosphatidylinositol Deficiency Disorders","volume":"95","author":"Nguyen","year":"2019","journal-title":"Clin. Genet."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2775","DOI":"10.1093\/brain\/awae056","article-title":"The Clinical and Genetic Spectrum of Inherited Glycosylphosphatidylinositol Deficiency Disorders","volume":"147","author":"Sidpra","year":"2024","journal-title":"Brain"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"17028","DOI":"10.1038\/nrdp.2017.28","article-title":"Paroxysmal Nocturnal Haemoglobinuria","volume":"3","author":"Hill","year":"2017","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"446","DOI":"10.3109\/10409238.2013.831024","article-title":"Gpi Transamidase and Gpi Anchored Proteins: Oncogenes and Biomarkers for Cancer","volume":"48","author":"Gamage","year":"2013","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1286","DOI":"10.1074\/mcp.M600035-MCP200","article-title":"Identification and Stoichiometry of Glycosylphosphatidylinositol-Anchored Membrane Proteins of the Human Malaria Parasite Plasmodium falciparum","volume":"5","author":"Gilson","year":"2006","journal-title":"Mol. Cell. Proteom."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nchembio.75","article-title":"Synthetic GPI Array to Study Antitoxic Malaria Response","volume":"4","author":"Kamena","year":"2008","journal-title":"Nat. Chem. Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"107557","DOI":"10.1016\/j.jbc.2024.107557","article-title":"The Major Surface Protein of Malaria Sporozoites Is GPI-Anchored to the Plasma Membrane","volume":"300","author":"Nagar","year":"2024","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2799","DOI":"10.1242\/jcs.112.17.2799","article-title":"The Structure, Biosynthesis and Functions of Glycosylphosphatidylinositol Anchors, and the Contributions of Trypanosome Research","volume":"112","author":"Ferguson","year":"1999","journal-title":"J. Cell Sci."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1016\/j.pt.2023.08.004","article-title":"Trypanosomes as a Magnifying Glass for Cell and Molecular Biology","volume":"39","author":"Speijer","year":"2023","journal-title":"Trends Parasitol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1038\/s41580-023-00616-9","article-title":"New Frontiers in Quality Control: The Case of GPI-Anchored Proteins","volume":"24","author":"Lemus","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nrm1052","article-title":"Quality Control in the Endoplasmic Reticulum","volume":"4","author":"Ellgaard","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1146\/annurev-arplant-042817-040331","article-title":"Protein Quality Control in the Endoplasmic Reticulum of Plants","volume":"69","author":"Strasser","year":"2018","journal-title":"Annu. Rev. Plant Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1016\/j.molcel.2022.03.025","article-title":"Reshaping Endoplasmic Reticulum Quality Control through the Unfolded Protein Response","volume":"82","author":"Wiseman","year":"2022","journal-title":"Mol. Cell"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"a041247","DOI":"10.1101\/cshperspect.a041247","article-title":"Endoplasmic Reticulum-Associated Protein Degradation","volume":"14","author":"Krshnan","year":"2022","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/s41580-023-00633-8","article-title":"Mechanisms of Substrate Processing during ER-Associated Protein Degradation","volume":"24","author":"Christianson","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1080\/10409238.2019.1610351","article-title":"Proteasomal and Lysosomal Clearance of Faulty Secretory Proteins: ER-Associated Degradation (ERAD) and ER-to-Lysosome-Associated Degradation (ERLAD) Pathways","volume":"54","author":"Fregno","year":"2019","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"102074","DOI":"10.1016\/j.ceb.2022.02.008","article-title":"Protein Quality Control at the Golgi","volume":"75","author":"Schwabl","year":"2022","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1083\/jcb.135.3.623","article-title":"A Pathway for Targeting Soluble Misfolded Proteins to the Yeast Vacuole","volume":"135","author":"Hong","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1091\/mbc.e09-10-0910","article-title":"Evasion of Endoplasmic Reticulum Surveillance Makes Wsc1p an Obligate Substrate of Golgi Quality Control","volume":"21","author":"Wang","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"EMBJ2018101433","DOI":"10.15252\/embj.2018101433","article-title":"Endosome and Golgi-associated Degradation (EGAD) of Membrane Proteins Regulates Sphingolipid Metabolism","volume":"38","author":"Schmidt","year":"2019","journal-title":"EMBO J."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/s41467-019-14038-9","article-title":"Golgi Organization Is Regulated by Proteasomal Degradation","volume":"11","author":"Benyair","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1083\/jcb.201312042","article-title":"ER-Associated Degradation: Protein Quality Control and Beyond","volume":"204","author":"Ruggiano","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_86","first-page":"158488","article-title":"Lipids and Their (Un)Known Effects on ER-Associated Protein Degradation (ERAD)","volume":"1865","author":"Goder","year":"2019","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Biol. Lipids"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Kumari, D., and Brodsky, J.L. (2021). The Targeting of Native Proteins to the Endoplasmic Reticulum-Associated Degradation (Erad) Pathway: An Expanding Repertoire of Regulated Substrates. Biomolecules, 11.","DOI":"10.3390\/biom11081185"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1083\/jcb.200106123","article-title":"Distinct Retrieval and Retention Mechanisms Are Required for the Quality Control of Endoplasmic Reticulum Protein Folding","volume":"155","author":"Vashist","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2296","DOI":"10.1091\/mbc.E19-01-0069","article-title":"Protein Folding State-Dependent Sorting at the Golgi Apparatus","volume":"30","author":"Hellerschmied","year":"2019","journal-title":"Mol. Biol. Cell"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.devcel.2011.05.015","article-title":"The ESCRT Pathway","volume":"21","author":"Henne","year":"2011","journal-title":"Dev. Cell"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1046\/j.1432-1327.1999.00176.x","article-title":"Ligand Recognition and Domain Structure of Vps10p, a Vacuolar Protein Sorting Receptor in Saccharomyces Cerevisiae","volume":"260","author":"Emr","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1534\/genetics.112.143487","article-title":"The Endosomal Protein-Sorting Receptor Sortilin Has a Role in Trafficking \u03b1-1 Antitrypsin","volume":"192","author":"Gelling","year":"2012","journal-title":"Genetics"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1186\/s12934-014-0125-0","article-title":"Secretion of a Foreign Protein from Budding Yeasts Is Enhanced by Cotranslational Translocation and by Suppression of Vacuolar Targeting","volume":"13","author":"Fitzgerald","year":"2014","journal-title":"Microb. Cell Fact."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"4025","DOI":"10.1016\/j.cub.2021.06.078","article-title":"Post-ER Degradation of Misfolded GPI-Anchored Proteins Is Linked with Microautophagy","volume":"31","author":"Lemus","year":"2021","journal-title":"Curr. Biol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/j.devcel.2015.03.007","article-title":"A Family of Tetraspans Organizes Cargo for Sorting into Multivesicular Bodies","volume":"33","author":"MacDonald","year":"2015","journal-title":"Dev. Cell"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1002\/j.1460-2075.1995.tb07119.x","article-title":"The Absence of Emp24p, a Component of ER-Derived COPII-Coated Vesicles, Causes a Defect in Transport of Selected Proteins to the Golgi","volume":"14","author":"Schimmoller","year":"1995","journal-title":"Embo J."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1083\/jcb.148.5.925","article-title":"The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum-Derived Vesicles","volume":"148","author":"Muniz","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1042\/BJ20070234","article-title":"Mammalian GPI-Anchored Proteins Require P24 Proteins for Their Efficient Transport from the ER to the Plasma Membrane","volume":"409","author":"Takida","year":"2008","journal-title":"Biochem. J."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Lopez, S., Perez-Linero, A.M., Manzano-Lopez, J., Sabido-Bozo, S., Cortes-Gomez, A., Rodriguez-Gallardo, S., Aguilera-Romero, A., Goder, V., and Mu\u00f1iz, M. (2020). Dual Independent Roles of the P24 Complex in Selectivity of Secretory Cargo Export from the Endoplasmic Reticulum. Cells, 9.","DOI":"10.3390\/cells9051295"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1104\/pp.20.00880","article-title":"P24 Family Proteins Are Involved in Transport to the Plasma Membrane of Gpi-Anchored Proteins in Plants","volume":"184","author":"Vieira","year":"2020","journal-title":"Plant Physiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"105016","DOI":"10.1016\/j.jbc.2023.105016","article-title":"Identification of the Glycosylphosphatidylinositol-Specific Phospholipase A2 (GPI-PLA2) That Mediates GPI Fatty Acid Remodeling in Trypanosoma brucei","volume":"299","author":"Ji","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_102","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":"ref_103","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1093\/plphys\/kiab384","article-title":"AtPGAP1 Functions as a GPI Inositol-Deacylase Required for Efficient Transport of GPI-Anchored Proteins","volume":"187","author":"Ma","year":"2021","journal-title":"Plant Physiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"18766","DOI":"10.1016\/S0021-9258(18)37349-6","article-title":"Lipid Analysis of the Glycoinositol Phospholipid Membrane Anchor of Human Erythrocyte Acetylcholinesterase. Palmitoylation of Inositol Results in Resistance to Phosphatidylinositol-Specific Phospholipase C","volume":"263","author":"Roberts","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"5253","DOI":"10.1091\/mbc.e06-08-0715","article-title":"PER1 Is Required for GPI-Phospholipase A(2) Activity and Involved in Lipid Remodeling of GPI-Anchored Proteins","volume":"17","author":"Fujita","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2636","DOI":"10.1091\/mbc.e06-02-0104","article-title":"GUP1 of Saccharomyces Cerevisiae Encodes an O-Acyltransferase Involved in Remodeling of the GPI Anchor","volume":"17","author":"Bosson","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"4304","DOI":"10.1091\/mbc.e07-05-0482","article-title":"Saccharomyces Cerevisiae CWH43 Is Involved in the Remodeling of the Lipid Moiety of GPI Anchors to Ceramides","volume":"18","author":"Umemura","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1194\/jlr.R063313","article-title":"Biosynthesis of GPI-Anchored Proteins: Special Emphasis on GPI Lipid Remodeling","volume":"57","author":"Kinoshita","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_109","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":"ref_110","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.cub.2014.11.039","article-title":"COPII Coat Composition Is Actively Regulated by Luminal Cargo Maturation","volume":"25","author":"Martin","year":"2015","journal-title":"Curr. Biol."},{"key":"ref_111","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":"ref_112","doi-asserted-by":"crossref","first-page":"2924","DOI":"10.1091\/mbc.e11-04-0294","article-title":"The Yeast P24 Complex Regulates GPI-Anchored Protein Transport and Quality Control by Monitoring Anchor Remodeling","volume":"22","author":"Castillon","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"8237","DOI":"10.1126\/sciadv.aba8237","article-title":"Ceramide Chain Length-Dependent Protein Sorting into Selective Endoplasmic Reticulum Exit Sites","volume":"6","author":"Kurokawa","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"110768","DOI":"10.1016\/j.celrep.2022.110768","article-title":"Quality-Controlled Ceramide-Based GPI-Anchored Protein Sorting into Selective ER Exit Sites","volume":"39","author":"Ikeda","year":"2022","journal-title":"Cell Rep."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1093\/jb\/mvm249","article-title":"O-Mannosylation Is Required for Degradation of the Endoplasmic Reticulum-Associated Degradation Substrate Gas1*p via the Ubiquitin\/Proteasome Pathway in Saccharomyces Cerevisiae","volume":"143","author":"Hirayama","year":"2008","journal-title":"J. Biochem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"3463","DOI":"10.1091\/mbc.e08-01-0087","article-title":"Retrotranslocation of Prion Proteins from the Endoplasmic Reticulum by Preventing GPI Signal Transamidation","volume":"19","author":"Ashok","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/j.cell.2014.06.026","article-title":"ER Stress-Induced Clearance of Misfolded GPI-Anchored Proteins via the Secretory Pathway","volume":"158","author":"Ajinkya","year":"2014","journal-title":"Cell"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1083\/jcb.201602010","article-title":"Limited ER Quality Control for GPI-Anchored Proteins","volume":"213","author":"Sikorska","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Ashok, A., and Hegde, R.S. (2009). Selective Processing and Metabolism of Disease-Causing Mutant Prion Proteins. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000479"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1242\/jcs.072181","article-title":"Protein O-Mannosyltransferases Participate in ER Protein Quality Control","volume":"124","author":"Goder","year":"2011","journal-title":"J. Cell Sci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1091\/mbc.e05-05-0443","article-title":"Inositol Deacylation by Bst1p Is Required for the Quality Control of Glycosylphosphatidylinositol-Anchored Proteins","volume":"17","author":"Fujita","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1091\/mbc.12.4.1093","article-title":"O-Mannosylation Protects Mutant Alpha-Factor Precursor from Endoplasmic Reticulum-Associated Degradation","volume":"12","author":"Harty","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1126\/science.1234055","article-title":"Futile Protein Folding Cycles in the ER Are Terminated by the Unfolded Protein O-Mannosylation Pathway","volume":"340","author":"Xu","year":"2013","journal-title":"Science"},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Lemus, L., Meyer, H., Rodr\u00edguez-Rosado, A.I., Schuldiner, M., and Goder, V. (EMBO J., 2025). O-Mannosylation of Misfolded ER Proteins Promotes ERAD, EMBO J., in press.","DOI":"10.1038\/s44318-025-00647-2"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1091\/mbc.e06-08-0664","article-title":"The Vacuolar Transporter Chaperone (VTC) Complex Is Required for Microautophagy","volume":"18","author":"Uttenweiler","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1083\/jcb.201404115","article-title":"A Sterol-Enriched Vacuolar Microdomain Mediates Stationary Phase Lipophagy in Budding Yeast","volume":"206","author":"Wang","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"e25960","DOI":"10.7554\/eLife.25960","article-title":"Niemann-Pick Type C Proteins Promote Microautophagy by Expanding Raft-like Membrane Domains in the Yeast Vacuole","volume":"6","author":"Tsuji","year":"2017","journal-title":"eLife"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1080\/15548627.2021.1971929","article-title":"Pep4-Dependent Microautophagy Is Required for Post-ER Degradation of GPI-Anchored Proteins","volume":"18","author":"Lemus","year":"2022","journal-title":"Autophagy"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"21732","DOI":"10.1074\/jbc.M213247200","article-title":"Mutant PrP Is Delayed in Its Exit from the Endoplasmic Reticulum, but Neither Wild-Type nor Mutant PrP Undergoes Retrotranslocation Prior to Proteasomal Degradation","volume":"278","author":"Drisaldi","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"4550","DOI":"10.1038\/sj.emboj.7600462","article-title":"Protection from Cytosolic Prion Protein Toxicity by Modulation of Protein Translocation","volume":"23","author":"Rane","year":"2004","journal-title":"EMBO J."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.devcel.2008.06.015","article-title":"Reduced Translocation of Nascent Prion Protein During ER Stress Contributes to Neurodegeneration","volume":"15","author":"Rane","year":"2008","journal-title":"Dev. Cell"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1083\/jcb.200911115","article-title":"Signal Sequence Insufficiency Contributes to Neurodegeneration Caused by Transmembrane Prion Protein","volume":"188","author":"Rane","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2363","DOI":"10.1080\/15548627.2020.1826691","article-title":"Membrane Dynamics and Protein Targets of Lipid Droplet Microautophagy during ER Stress-Induced Proteostasis in the Budding Yeast, Saccharomyces Cerevisiae","volume":"17","author":"Garcia","year":"2020","journal-title":"Autophagy"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"14955","DOI":"10.1073\/pnas.011578098","article-title":"Wild-Type PrP and a Mutant Associated with Prion Disease Are Subject to Retrograde Transport and Proteasome Degradation","volume":"98","author":"Ma","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"5383","DOI":"10.1093\/emboj\/20.19.5383","article-title":"Proteasomes and Ubiquitin Are Involved in the Turnover of the Wild-Type Prion Protein","volume":"20","author":"Yedidia","year":"2001","journal-title":"Embo J."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"e46740","DOI":"10.7554\/eLife.46740","article-title":"Misfolded GPI-Anchored Proteins Are Escorted through the Secretory Pathway by ER-Derived Factors","volume":"8","author":"Zavodszky","year":"2019","journal-title":"eLife"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"e5511","DOI":"10.21769\/BioProtoc.5511","article-title":"Monitoring Endocytosis of Integral Membrane Proteins Using Western Blot-Based Detection of Biotinylated Antibody Uptake","volume":"15","author":"Graninger","year":"2025","journal-title":"Bio. Protoc."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Ronzier, E., and Satpute-Krishnan, P. (2025). TMED9 Coordinates the Clearance of Misfolded GPI-Anchored Proteins out of the ER and into the Golgi. PLoS Biol., 23.","DOI":"10.1371\/journal.pbio.3003084"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"e202108160","DOI":"10.1083\/jcb.202108160","article-title":"Competition for Calnexin Binding Regulates Secretion and Turnover of Misfolded GPI-Anchored Proteins","volume":"222","author":"Cheatham","year":"2023","journal-title":"J. Cell Biol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1007\/s00415-002-0896-9","article-title":"Mutations of the Prion Protein Gene Phenotypic Spectrum","volume":"249","author":"Trabattoni","year":"2002","journal-title":"J. Neurol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.autrev.2006.09.008","article-title":"The Role of Complement Regulatory Proteins (CD55 and CD59) in the Pathogenesis of Autoimmune Hemocytopenias","volume":"6","author":"Llorente","year":"2007","journal-title":"Autoimmun. Rev."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"11","DOI":"10.4161\/pri.27892","article-title":"The GPI-Anchoring of PrP: Implications in Sorting and Pathogenesis","volume":"8","author":"Puig","year":"2014","journal-title":"Prion"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1083\/jcb.201706135","article-title":"N-Glycan\u2013Dependent Protein Folding and Endoplasmic Reticulum Retention Regulate GPI-Anchor Processing","volume":"217","author":"Liu","year":"2018","journal-title":"J. Cell Biol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"16393","DOI":"10.1074\/jbc.RA120.015577","article-title":"Calnexin Mediates the Maturation of GPI-Anchors through ER Retention","volume":"295","author":"Guo","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1038\/s41467-023-44568-2","article-title":"Molecular Basis of the Inositol Deacylase PGAP1 Involved in Quality Control of GPI-AP Biogenesis","volume":"15","author":"Hong","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1007\/s00497-020-00395-9","article-title":"Bridging the GAPs in Plant Reproduction: A Comparison of Plant and Animal GPI-Anchored Proteins","volume":"33","author":"Desnoyer","year":"2020","journal-title":"Plant Reprod."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"4778","DOI":"10.1093\/plcell\/koac257","article-title":"Glycosylphosphatidylinositol Anchor Lipid Remodeling Directs Proteins to the Plasma Membrane and Governs Cell Wall Mechanics","volume":"34","author":"Xu","year":"2022","journal-title":"Plant Cell"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1878","DOI":"10.1093\/plphys\/kiab181","article-title":"Proper Protein Folding in the Endoplasmic Reticulum Is Required for Attachment of a Glycosylphosphatidylinositol Anchor in Plants","volume":"186","author":"Shin","year":"2021","journal-title":"Plant Physiol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1093\/plphys\/kiab257","article-title":"Dropping Anchor: Stringent Quality Control Prevents GPI Anchoring of Severely Misfolded Proteins in Plants","volume":"186","author":"Skelly","year":"2021","journal-title":"Plant Physiol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1042\/bj3350681","article-title":"Glycosylphosphatidylinositol-Dependent Secretory Transport in Trypanosoma brucei","volume":"335","author":"McDowell","year":"1998","journal-title":"Biochem. J."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"4285","DOI":"10.1093\/emboj\/16.14.4285","article-title":"Expression of Bloodstream Variant Surface Glycoproteins in Procyclic Stage Trypanosoma brucei: Role of GPI Anchors in Secretion","volume":"16","author":"Bangs","year":"1997","journal-title":"EMBO J."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2397","DOI":"10.1091\/mbc.E18-06-0380","article-title":"Endoplasmic Reticulum-Associated Degradation and Disposal of Misfolded GPI-Anchored Proteins in Trypanosoma brucei","volume":"29","author":"Tiengwe","year":"2018","journal-title":"Mol. Biol. Cell"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"12147","DOI":"10.1074\/jbc.275.16.12147","article-title":"A Role for the Dynamic Acylation of a Cluster of Cysteine Residues in Regulating the Activity of the Glycosylphosphatidylinositol-Specific Phospholipase C of Trypanosoma brucei","volume":"275","author":"Nolan","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.cell.2015.11.051","article-title":"Extracellular Vesicles from Trypanosoma brucei Mediate Virulence Factor Transfer and Cause Host Anemia","volume":"164","author":"Szempruch","year":"2016","journal-title":"Cell"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1128\/mBio.01725-21","article-title":"Turnover of Variant Surface Glycoprotein in Trypanosoma brucei Is a Bimodal Process","volume":"12","author":"Garrison","year":"2021","journal-title":"mBio"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1800181","DOI":"10.1002\/bies.201800181","article-title":"Evolution of Antigenic Variation in African Trypanosomes: Variant Surface Glycoprotein Expression, Structure, and Function","volume":"40","author":"Bangs","year":"2018","journal-title":"Bioessays"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/j.molcel.2017.06.012","article-title":"Activation of the Unfolded Protein Response by Lipid Bilayer Stress","volume":"67","author":"Halbleib","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.molcel.2018.07.019","article-title":"Integrated Functions of Membrane Property Sensors and a Hidden Side of the Unfolded Protein Response","volume":"71","author":"Covino","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_159","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":"ref_160","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1083\/jcb.200406136","article-title":"XBP1: A Link between the Unfolded Protein Response, Lipid Biosynthesis, and Biogenesis of the Endoplasmic Reticulum","volume":"167","author":"Sriburi","year":"2004","journal-title":"J. Cell Biol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/s41467-020-14678-2","article-title":"Cross-Talks of Glycosylphosphatidylinositol Biosynthesis with Glycosphingolipid Biosynthesis and ER-Associated Degradation","volume":"11","author":"Wang","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"37","DOI":"10.2174\/156652406775574578","article-title":"Stressing out the ER: A Role of the Unfolded Protein Response in Prion-Related Disorders","volume":"6","author":"Hetz","year":"2006","journal-title":"Curr. Mol. Med."},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Field, M.C., Sergeenko, T., Wang, Y.-N., B\u00f6 Hm, S., and Carrington, M. (2010). Chaperone Requirements for Biosynthesis of the Trypanosome Variant Surface Glycoprotein. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0008468"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1111\/cmi.12605","article-title":"Variant Surface Glycoprotein, Transferrin Receptor, and ERAD in Trypanosoma brucei","volume":"18","author":"Tiengwe","year":"2016","journal-title":"Cell. Microbiol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"11676","DOI":"10.1073\/pnas.0704862104","article-title":"The Evolution of N-Glycan-Dependent Endoplasmic Reticulum Quality Control Factors for Glycoprotein Folding and Degradation","volume":"104","author":"Banerjee","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"35929","DOI":"10.1074\/jbc.M509130200","article-title":"Deletion of the Glucosidase II Gene in Trypanosoma brucei Reveals Novel N-Glycosylation Mechanisms in the Biosynthesis of Variant Surface Glycoprotein","volume":"280","author":"Jones","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1093\/glycob\/cws003","article-title":"The Lipid-Linked Oligosaccharide Donor Specificities of Trypanosoma brucei Oligosaccharyltransferases","volume":"22","author":"Izquierdo","year":"2012","journal-title":"Glycobiology"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0092-8674(90)90241-6","article-title":"Fatty Acid Remodeling: A Novel Reaction Sequence in the Biosynthesis of Trypanosome Glycosyl Phosphatidylinositol Membrane Anchors","volume":"62","author":"Masterson","year":"1990","journal-title":"Cell"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/14\/6316\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,18]],"date-time":"2026-07-18T04:15:57Z","timestamp":1784348157000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/14\/6316"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,16]]},"references-count":168,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["ijms27146316"],"URL":"https:\/\/doi.org\/10.3390\/ijms27146316","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,16]]}}}