PIGT (GPI-anchor transamidase component PIG-T) is one of the five subunits of the glycosylphosphatidylinositol-anchor transamidase (GPI-T) complex, an endoplasmic reticulum membrane enzyme complex that attaches the pre-assembled GPI anchor to the C-terminus of GPI-anchored proteins after cleaving their C-terminal GPI-attachment signal peptide. The complex comprises the catalytic subunit PIGK (GPI8) together with GPAA1, PIGS, PIGU and PIGT as an equimolar heteropentamer. PIGT is a single-pass type I ER membrane glycoprotein that acts as a required structural subunit; it forms an interchain disulfide bond with the catalytic PIGK/GPI8 (PIGT Cys182 to PIGK Cys92) and stabilises and holds the complex together, and it also contributes to binding of the GPI lipid substrate. PIGT itself is not an independent enzyme, the transamidation catalysis residing in PIGK. Biallelic loss-of-function variants in PIGT cause the inherited GPI deficiency multiple congenital anomalies-hypotonia-seizures syndrome 3 (MCAHS3), and germline plus somatic PIGT variants can produce a paroxysmal nocturnal hemoglobinuria-like phenotype (PNH2).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016255 attachment of GPI anchor to protein | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) annotation to the core biological process of PIGT and its orthologues, the attachment of GPI anchors to proteins. This is the well-established, correct core function of the gene. Reason: This IBA annotation correctly captures PIGT's core biological role as a subunit of the GPI transamidase, which attaches pre-assembled GPI to proteins in the ER. It is supported by experimental knockout data and by the entire structural/biochemical literature. Supporting Evidence: PMID:11483512 PIG-S and PIG-T knockout cells were defective in transfer of GPI PMID:34576938 Attachment of GPI to proteins is mediated by the GPI-transamidase (GPI-TA) |
| GO:0042765 GPI-anchor transamidase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) annotation placing PIGT as a part of the GPI-anchor transamidase complex, the correct and core cellular component for this gene. Reason: PIGT is a bona fide subunit of the heteropentameric GPI-T complex (PIGK, GPAA1, PIGS, PIGU, PIGT). This is directly established experimentally and structurally. Supporting Evidence: PMID:11483512 PIG-S and PIG-T form a protein complex with GAA1 and GPI8 PMID:35551457 revealing an equimolar |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Electronic annotation (from UniProt Subcellular Location mapping) to the ER membrane, the correct localisation of PIGT and the GPI-T complex. Reason: PIGT is a single-pass type I ER membrane protein; the GPI-T complex is an ER membrane complex. This IEA mapping is fully consistent with experimental localisation data. Supporting Evidence: PMID:15713669 PIG-T is a type I PMID:35165458 Attaching GPI to the protein in the endoplasmic reticulum (ER) is catalyzed by |
| GO:0016255 attachment of GPI anchor to protein | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic (combined IEA methods, via mouse ortholog and InterPro PIG-T domain) annotation to GPI anchor attachment, the core BP of PIGT. Reason: This electronic annotation agrees with the IBA and multiple experimental annotations for the same process. It is correct at an appropriate level of specificity. Supporting Evidence: PMID:34576938 Attachment of GPI to proteins is mediated by the GPI-transamidase (GPI-TA) |
| GO:0042765 GPI-anchor transamidase complex | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic (combined IEA methods) annotation to the GPI-anchor transamidase complex, agreeing with the experimental IDA/IBA complex annotations. Reason: Correct complex membership, redundant with but consistent with the experimental and phylogenetic annotations of the same complex. Supporting Evidence: PMID:34576938 GPI-TA consists of five subunits: PIGK, GPAA1, PIGT, PIGS, and |
| GO:0005515 protein binding | IPI PMID:11483512 PIG-S and PIG-T, essential for GPI anchor attachment to prot... | MARK AS OVER ANNOTATED | Summary: IntAct IPI capturing PIGT physical interactions with other GPI-T subunits (GPAA1/PIGK/PIGS). Bare 'protein binding' is uninformative about the actual molecular function. Reason: The interaction is real and biologically meaningful, but the generic 'protein binding' term conveys no functional information beyond what is already captured more informatively by the GPI-anchor transamidase complex (GO:0042765) membership. Per curation guidance, bare protein binding is discouraged in favour of a more specific term. Retained rather than removed because it reflects a genuine curated interaction. Supporting Evidence: PMID:11483512 PIG-S and PIG-T form a protein complex with GAA1 and GPI8 |
| GO:0005515 protein binding | IPI PMID:12802054 Human PIG-U and yeast Cdc91p are the fifth subunit of GPI tr... | MARK AS OVER ANNOTATED | Summary: IntAct IPI recording PIGT interaction with GPI-T subunits identified during characterisation of PIG-U as the fifth subunit. Bare 'protein binding' is uninformative. Reason: Genuine interaction within the GPI-T complex, but 'protein binding' is too generic; the informative content is already captured by GO:0042765. Retained as a valid curated interaction rather than removed. Supporting Evidence: PMID:12802054 The mammalian GPI transamidase is a |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MARK AS OVER ANNOTATED | Summary: IntAct IPI derived from the BioPlex 2.0 large-scale affinity-purification interactome. Bare 'protein binding' with no specific functional information. Reason: High-throughput interactome data supporting membership in a protein community, but the generic 'protein binding' term is uninformative and redundant with the more specific complex annotation (GO:0042765). Supporting Evidence: PMID:28514442 networks of protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: IntAct IPI derived from the BioPlex 3.0 proteome-scale interactome. Bare 'protein binding' term, uninformative about molecular function. Reason: Large-scale interactome evidence; generic and redundant with the GPI-anchor transamidase complex annotation. Retained as valid interaction data. Supporting Evidence: PMID:33961781 Thousands of interactions assemble proteins into modules |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MARK AS OVER ANNOTATED | Summary: IntAct IPI from a multimodal cell-map/interactome study. Bare 'protein binding' term without specific molecular-function content. Reason: Systematic interactome mapping; genuine but generic. The informative function is captured by complex membership (GO:0042765). Supporting Evidence: PMID:40205054 Multimodal cell maps as a foundation for structural and functional genomics |
| GO:0006506 GPI anchor biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: Electronic annotation (UniPathway mapping, UPA00196 glycosylphosphatidylinositol-anchor biosynthesis) to the GPI anchor biosynthetic process. PIGT participates in the final transamidation/attachment step of this pathway as part of GPI-T. Reason: PIGT participates in the terminal step of GPI anchor biosynthesis (attachment of the anchor to protein). This pathway-level BP is correct and consistent with the UniProt PATHWAY annotation. Supporting Evidence: PMID:35551457 covalent attachment of GPI at the new carboxyl terminus are catalyzed by an |
| GO:0005789 endoplasmic reticulum membrane | NAS PMID:12802054 Human PIG-U and yeast Cdc91p are the fifth subunit of GPI tr... | ACCEPT | Summary: Author-statement (NAS, ComplexPortal) annotation to the ER membrane, matching the established localisation of PIGT within the ER-membrane GPI-T complex. Reason: Correct localisation. The GPI transamidase is an ER-membrane complex and PIGT is an integral ER membrane protein. Supporting Evidence: PMID:12802054 posttranslationally attached to the PMID:15713669 PIG-T is a type I |
| GO:0016255 attachment of GPI anchor to protein | NAS PMID:12802054 Human PIG-U and yeast Cdc91p are the fifth subunit of GPI tr... | ACCEPT | Summary: Author-statement (NAS, ComplexPortal) annotation to GPI anchor attachment, the core BP of the GPI-T complex to which PIGT belongs. Reason: Correct core process; redundant with but consistent with the IBA and IDA annotations for the same term. Supporting Evidence: PMID:12802054 carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a |
| GO:0042765 GPI-anchor transamidase complex | IPI PMID:12802054 Human PIG-U and yeast Cdc91p are the fifth subunit of GPI tr... | ACCEPT | Summary: IPI (ComplexPortal, CPX-6503) annotation placing PIGT in the GPI-anchor transamidase complex, based on affinity-purification of the complex. Reason: Directly supported complex membership; PIGT co-purifies with the other four GPI-T subunits. This is the core cellular component for PIGT. Supporting Evidence: PMID:12802054 The mammalian GPI transamidase is a |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:35165458 Structure of human glycosylphosphatidylinositol transamidase... | ACCEPT | Summary: IDA (cryo-EM structure of the human GPI-T complex) annotation to GPI anchored protein biosynthesis, the overall process to which the PIGT-containing complex contributes. Reason: The structure confirms PIGT as a subunit of the complex that catalyses GPI-AP biogenesis. This BP is correct; it is the pathway output of GPI anchor attachment, so somewhat broader/less specific than GO:0016255 but valid. Supporting Evidence: PMID:35165458 which is essential for |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:35551457 Molecular insights into biogenesis of glycosylphosphatidylin... | ACCEPT | Summary: IDA (2.53-Angstrom cryo-EM structure of the human GPI-T heteropentamer) annotation to GPI anchored protein biosynthesis. Reason: Structure of the GPI-T complex directly implicates PIGT in GPI-AP biogenesis. Correct process-level annotation. Supporting Evidence: PMID:35551457 covalent attachment of GPI at the new carboxyl terminus are catalyzed by an |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:28327575 Analysis of exome data for 4293 trios suggests GPI-anchor bi... | ACCEPT | Summary: IDA annotation to GPI anchor attachment based on functional characterisation of MCAHS3 patient variants that impair GPI-anchored protein surface expression. Reason: Patient-variant and rescue assays demonstrate that PIGT function is required for attachment of GPI anchors to proteins. Core BP, correctly annotated. Supporting Evidence: PMID:28327575 Mutations in 18 genes that encode |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:36970549 Case report: Functional analysis of the p.Arg507Trp variant ... | ACCEPT | Summary: IDA annotation to GPI anchor attachment from FACS analysis of PIGT-knockout cells rescued with wild-type versus p.Arg507Trp mutant cDNA, showing the variant reduces activity. Reason: Functional assay directly links PIGT to GPI anchor attachment activity; pathogenic variants reduce it. Core BP, correctly annotated. Supporting Evidence: PMID:36970549 leads to mildly reduced |
| GO:0016255 attachment of GPI anchor to protein | TAS PMID:37684232 Structures of liganded glycosylphosphatidylinositol transami... | ACCEPT | Summary: TAS annotation to GPI anchor attachment from the liganded GPI-T structural study describing the transamidation reaction catalysed by the complex. Reason: The GPI-T complex, of which PIGT is a subunit, replaces the signal peptide with GPI via transamidation. Correct core BP. Supporting Evidence: PMID:37684232 replaces it with GPI via a transamidation reaction |
| GO:0034235 GPI anchor binding | IDA PMID:11483512 PIG-S and PIG-T, essential for GPI anchor attachment to prot... | ACCEPT | Summary: IDA annotation that PIGT binds the GPI anchor. This is an informative molecular function for PIGT, which contributes lipid-substrate binding residues within the GPI-T complex. Reason: This is the most informative MF annotation present for PIGT and is retained. Subsequent cryo-EM structures corroborate that the GPI lipid substrate is bound in a composite cavity of the complex, with PIGT contributing binding residues (UniProt BINDING sites 461/521/523/527). Per policy, an experimental IDA whose full text is unavailable to me is not removed; the function is biologically sound. Supporting Evidence: PMID:35551457 endogenous GPI in the structure defines a composite cavity for the lipid |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:11483512 PIG-S and PIG-T, essential for GPI anchor attachment to prot... | ACCEPT | Summary: IDA annotation to GPI anchored protein biosynthesis based on PIG-T knockout cells being defective in transfer of GPI to proteins. Reason: Knockout data directly implicate PIGT in GPI-AP biogenesis. Correct process annotation (pathway output of GPI anchor attachment). Supporting Evidence: PMID:11483512 PIG-S and PIG-T knockout cells were defective in transfer of GPI |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:12582175 Two subunits of glycosylphosphatidylinositol transamidase, G... | ACCEPT | Summary: IDA annotation to GPI anchored protein biosynthesis from the study of the functionally important PIG-T/GPI8 intermolecular disulfide bond. Reason: PIGT is required for full transamidase activity of the complex that produces GPI-anchored proteins. Correct process annotation. Supporting Evidence: PMID:12582175 required for full transamidase activity |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:28327575 Analysis of exome data for 4293 trios suggests GPI-anchor bi... | ACCEPT | Summary: IDA annotation to GPI anchored protein biosynthesis from functional analysis of MCAHS3 patient variants reducing GPI-AP surface display. Reason: Variant/rescue data show PIGT is needed for GPI-AP biogenesis. Correct process annotation. Supporting Evidence: PMID:28327575 Mutations in 18 genes that encode |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:34576938 Functional Analysis of the GPI Transamidase Complex by Scree... | ACCEPT | Summary: IDA annotation to GPI anchored protein biosynthesis from functional analysis of amino-acid mutations across the five GPI-TA subunits including PIGT. Reason: Mutational screening confirms PIGT function within the GPI-TA complex that biosynthesises GPI-anchored proteins. Correct process annotation. Supporting Evidence: PMID:34576938 the absence of any subunit leads to the loss of activity |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:36970549 Case report: Functional analysis of the p.Arg507Trp variant ... | ACCEPT | Summary: IDA annotation to GPI anchored protein biosynthesis from knockout-rescue functional analysis of the p.Arg507Trp PIGT variant. Reason: Functional assay implicates PIGT in GPI-AP biogenesis. Correct process annotation. Supporting Evidence: PMID:36970549 leads to mildly reduced |
| GO:0180046 GPI anchored protein biosynthesis | IDA PMID:37684232 Structures of liganded glycosylphosphatidylinositol transami... | ACCEPT | Summary: IDA annotation to GPI anchored protein biosynthesis from the liganded GPI-T structural study. Reason: The GPI-T structure, including PIGT, directly informs the biogenesis of GPI-anchored proteins. Correct process annotation. Supporting Evidence: PMID:37684232 replaces it with GPI via a transamidation reaction |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:12802054 Human PIG-U and yeast Cdc91p are the fifth subunit of GPI tr... | ACCEPT | Summary: IDA annotation to GPI anchor attachment from the characterisation of the five-subunit GPI transamidase complex. Reason: The reconstituted five-subunit complex (including PIGT) performs GPI anchor attachment. Core BP, correctly annotated. Supporting Evidence: PMID:12802054 carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:34576938 Functional Analysis of the GPI Transamidase Complex by Scree... | ACCEPT | Summary: IDA annotation to GPI anchor attachment from mutational analysis of the GPI-TA complex subunits. Reason: Confirms PIGT contribution to GPI anchor attachment activity of the complex. Core BP, correctly annotated. Supporting Evidence: PMID:34576938 Attachment of GPI to proteins is mediated by the GPI-transamidase (GPI-TA) |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:37684232 Structures of liganded glycosylphosphatidylinositol transami... | ACCEPT | Summary: IDA annotation to GPI anchor attachment from the liganded GPI-T structures illuminating substrate recognition and transamidation. Reason: The complex containing PIGT attaches GPI to proprotein C-termini by transamidation. Core BP, correctly annotated. Supporting Evidence: PMID:37684232 replaces it with GPI via a transamidation reaction |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:37684232 Structures of liganded glycosylphosphatidylinositol transami... | ACCEPT | Summary: IDA (cryo-EM) annotation placing PIGT in the GPI-anchor transamidase complex, resolved as a heteropentamer with bound GPI/substrate. Reason: Structurally confirmed complex membership. Core cellular component for PIGT. Supporting Evidence: PMID:37684232 replaces it with GPI via a transamidation reaction |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:35165458 Structure of human glycosylphosphatidylinositol transamidase... | ACCEPT | Summary: IDA annotation to GPI anchor attachment from the first human GPI-T cryo-EM structure, which identified the PIGK catalytic triad and the GPI substrate cleft. Reason: The structure directly demonstrates how the PIGT-containing complex attaches GPI to proteins. Core BP, correctly annotated. Supporting Evidence: PMID:35165458 Attaching GPI to the protein in the endoplasmic reticulum (ER) is catalyzed by |
| GO:0016255 attachment of GPI anchor to protein | IDA PMID:35551457 Molecular insights into biogenesis of glycosylphosphatidylin... | ACCEPT | Summary: IDA annotation to GPI anchor attachment from the 2.53-Angstrom human GPI-T structure with endogenous GPI bound. Reason: Structure of the heteropentameric complex including PIGT elucidates GPI anchor attachment. Core BP, correctly annotated. Supporting Evidence: PMID:35551457 covalent attachment of GPI at the new carboxyl terminus are catalyzed by an |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:35165458 Structure of human glycosylphosphatidylinositol transamidase... | ACCEPT | Summary: IDA (cryo-EM) annotation placing PIGT in the GPI-anchor transamidase complex, composed of PIGK, PIGU, PIGT, PIGS and GPAA1. Reason: Structurally confirmed complex membership. Core cellular component. Supporting Evidence: PMID:35165458 The GPIT complex is known to be |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:35551457 Molecular insights into biogenesis of glycosylphosphatidylin... | ACCEPT | Summary: IDA (cryo-EM) annotation placing PIGT in the GPI-anchor transamidase complex, resolved as an equimolar heteropentamer. Reason: Structurally confirmed complex membership. Core cellular component. Supporting Evidence: PMID:35551457 revealing an equimolar |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:12582175 Two subunits of glycosylphosphatidylinositol transamidase, G... | ACCEPT | Summary: IDA annotation placing PIGT in the GPI transamidase complex, based on the demonstration that GPI8/PIGK and PIG-T form a functionally important disulfide bond within the multimeric complex. Reason: PIGT is a subunit that disulfide-links to catalytic PIGK; the intact complex is composed of five subunits. Core cellular component. Supporting Evidence: PMID:12582175 two subunits of mammalian GPI transamidase, GPI8 and PIG-T, form PMID:12582175 these five components are sufficient to |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:34576938 Functional Analysis of the GPI Transamidase Complex by Scree... | ACCEPT | Summary: IDA annotation placing PIGT in the GPI-anchor transamidase complex, from the purification and mutational analysis of the five-subunit GPI-TA. Reason: PIGT is one of the five subunits of the purified GPI-TA. Core cellular component. Supporting Evidence: PMID:34576938 GPI-TA consists of five subunits: PIGK, GPAA1, PIGT, PIGS, and |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:12802054 Human PIG-U and yeast Cdc91p are the fifth subunit of GPI tr... | ACCEPT | Summary: IDA annotation placing PIGT in the GPI-anchor transamidase complex, from affinity purification of the epitope-tagged complex containing PIG-U and PIGT. Reason: PIGT co-purifies as a subunit of the GPI transamidase complex. Core cellular component. Supporting Evidence: PMID:12802054 The mammalian GPI transamidase is a |
| GO:0042765 GPI-anchor transamidase complex | IDA PMID:11483512 PIG-S and PIG-T, essential for GPI anchor attachment to prot... | ACCEPT | Summary: IDA annotation placing PIGT in the GPI-anchor transamidase complex, from the original identification of PIG-S and PIG-T as subunits complexing with GAA1 and GPI8. Reason: Foundational experimental demonstration that PIGT is a subunit of the GPI transamidase complex and stabilises it. Core cellular component. Supporting Evidence: PMID:11483512 PIG-S and PIG-T form a protein complex with GAA1 and GPI8 PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8 |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: High-throughput (HDA) proteomics annotation to the generic 'membrane' term, from a membrane-proteome analysis of an NK-like cell line. Reason: PIGT is indeed a membrane protein, so the annotation is not wrong, but 'membrane' is far less specific than the well-supported ER membrane (GO:0005789) localisation. Kept as non-core given the more informative CC terms already present. Supporting Evidence: PMID:19946888 Defining the membrane proteome of NK cells |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-162836 | ACCEPT | Summary: TAS (Reactome) annotation to the ER membrane, from the uPAR GPI-attachment reaction catalysed by the ER-membrane GPI transamidase complex. Reason: Correct localisation consistent with all other CC evidence for PIGT and the GPI-T complex. Supporting Evidence: Reactome:R-HSA-162836 a complex of at least five proteins associated with the lumenal surface of the endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | NAS PMID:12052837 Structural requirements for the recruitment of Gaa1 into a f... | ACCEPT | Summary: Author-statement (NAS) annotation to the ER membrane, from the study of Gaa1 recruitment into the ER-localised GPI transamidase complex. Reason: Correct localisation; the GPI transamidase (including PIGT) is an ER-membrane complex. Supporting Evidence: PMID:12052837 Gaa1 is an endoplasmic |
| GO:0016255 attachment of GPI anchor to protein | TAS PMID:11483512 PIG-S and PIG-T, essential for GPI anchor attachment to prot... | ACCEPT | Summary: TAS annotation to GPI anchor attachment from the original PIG-S/PIG-T identification paper. Reason: PIG-T is essential for attachment of GPI anchors to proteins. Core BP, correctly annotated. Supporting Evidence: PMID:11483512 PIG-S and PIG-T knockout cells were defective in transfer of GPI |
| GO:0005515 protein binding | IPI PMID:15713669 Endoplasmic reticulum localization of Gaa1 and PIG-T, subuni... | MARK AS OVER ANNOTATED | Summary: IPI annotation of a PIGT interaction (with GPAA1/O43292) from the study of ER localisation of Gaa1 and PIG-T. Bare 'protein binding' term. Reason: Genuine interaction with a partner GPI-T subunit, but 'protein binding' is uninformative and redundant with the complex membership annotation (GO:0042765). Retained as a valid curated interaction. Supporting Evidence: PMID:15713669 subunits of the |
| GO:0042765 GPI-anchor transamidase complex | TAS PMID:15713669 Endoplasmic reticulum localization of Gaa1 and PIG-T, subuni... | ACCEPT | Summary: TAS annotation placing PIGT in the GPI transamidase complex, from the study of ER localisation of two of its subunits (Gaa1 and PIG-T). Reason: PIGT is described as one of the five subunits of the GPI transamidase complex. Core cellular component. Supporting Evidence: PMID:15713669 subunits of the |
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Download this section (compressed HTML)Q: Does PIGT contribute directly to GPI lipid-substrate recognition/binding beyond a purely structural role, and can its binding residues (e.g. positions 461/521/523/527) be functionally separated from its complex-stabilising function?
Q: How do specific MCAHS3 missense variants map onto the complex-stabilising versus substrate-binding roles of PIGT, and does this explain the mild-versus-severe epilepsy phenotype spectrum?
Experiment: Structure-guided mutagenesis of PIGT GPI-lipid-binding residues in a PIGT-knockout rescue system, measuring cell-surface GPI-anchored protein display (CD59/CD16b) versus complex assembly, to dissect PIGT's substrate-binding contribution from its structural/stabilising role.
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