The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The UniProt target Q9US48 (gaa1; SPAC1002.11) is annotated as “GPI transamidase component Gaa1” in Schizosaccharomyces pombe (strain 972). Direct S. pombe-specific biochemical/genetic literature for SPAC1002.11 was not retrieved in the accessible full-text corpus; therefore, species-specific functional statements are necessarily inferred by orthology to the conserved Gaa1/GPAA1 family, with explicit supporting evidence that a S. pombe Gaa1 ortholog is recognized in cross-species comparisons of function-critical motifs. Specifically, a cross-species alignment of the last transmembrane helix of Gaa1 orthologs explicitly includes Schizosaccharomyces pombe and highlights a conserved proline motif required for GPI recognition in the transamidase complex. (vainauskas2004aconservedproline pages 4-5)
GPI anchoring is a conserved eukaryotic post-translational modification that converts a secretory-pathway protein (a “preproprotein”) into a membrane-tethered protein by attaching a preassembled glycolipid (GPI) to the protein’s C-terminus. In the canonical reaction, GPI transamidase (GPI-T/GPIT) recognizes a C-terminal GPI signal sequence, cleaves the protein at the ω-site (the future C-terminus), and replaces the signal peptide with a GPI anchor, creating an amide (peptide) bond between the protein’s new C-terminal carboxyl at the ω-residue and an amine on the GPI anchor (commonly described as a terminal ethanolamine/phosphoethanolamine group). (vainauskas2002structuralrequirementsfor pages 1-1, gamage2013gpitransamidaseand pages 3-5, vainauskas2004aconservedproline pages 1-1)
This reaction occurs in the endoplasmic reticulum (ER) and is described as the final “commitment” step that produces a mature GPI-anchored protein. (vainauskas2002structuralrequirementsfor pages 1-1, gamage2013gpitransamidaseand pages 3-5)
Gaa1 (yeast nomenclature) / GPAA1 (metazoan nomenclature) is a conserved, multi-pass ER membrane component of GPI transamidase. Structure-function analyses in mammalian systems characterize Gaa1 as an ER-localized membrane glycoprotein with cytosolic N-terminus and luminal C-terminus, and a large luminal region critical for association with other GPI-T subunits. (vainauskas2002structuralrequirementsfor pages 1-1)
A key functional theme for Gaa1/GPAA1 across systems is coupling substrate recognition and GPI (lipid) recognition/presentation to the catalytic reaction performed by the transamidase complex. (vainauskas2002structuralrequirementsfor pages 1-1, vainauskas2004aconservedproline pages 1-1)
GPI transamidase recognizes a C-terminal signal with characteristic features: a short region surrounding the ω-site, a hydrophilic spacer, and a hydrophobic C-terminal tail. The ω-site (attachment residue) tends to be a small side chain; constraints at ω+1 and ω+2 are also strong (e.g., ω+2 often small), sometimes described as a “small amino acid domain.” (xu2022molecularinsightsinto pages 2-4, gamage2013gpitransamidaseand pages 3-5, vainauskas2004aconservedproline pages 1-1)
One mechanistic synthesis argues “only residues Ala, Asn, Asp, Cys, Gly, and Ser” are possible at the ω-site in typical substrates. (eisenhaber2014transamidasesubunitgaa1gpaa1 pages 2-4, eisenhaber2014transamidasesubunitgaa1gpaa1 pages 4-5)
Best-supported functional assignment (orthology-based): gaa1 encodes a GPI transamidase component (Gaa1/GPAA1 family) required for efficient attachment of GPI anchors to secretory proteins in the ER.
Evidence basis:
- GPI transamidase chemistry and the role of Gaa1-family proteins in substrate interactions are experimentally supported in mammalian systems: proproteins can bind Gaa1 even when the catalytic subunit Gpi8/PIGK is absent, consistent with a substrate-recruitment role for Gaa1. (vainauskas2002structuralrequirementsfor pages 1-1)
- The last transmembrane segment of Gaa1 is implicated in GPI recognition: truncations and point mutations (including a conserved proline) disrupt GPI co-precipitation while preserving assembly and proprotein binding, indicating a role in binding/presenting the lipid substrate. (vainauskas2004aconservedproline pages 1-1)
- Cross-species sequence analysis explicitly includes a Schizosaccharomyces pombe Gaa1 ortholog and shows conservation of the function-critical proline motif in the last TM segment, supporting that S. pombe gaa1/Q9US48 is a true family member with conserved mechanistic features. (vainauskas2004aconservedproline pages 4-5)
Important nuance / current uncertainty: In the literature, the precise catalytic assignment for GPAA1/Gaa1 has evolved. A 2022 near-atomic cryo-EM structure of human GPI-T supports PIGK as the catalytic cysteine protease (with an essential catalytic dyad) and provides evidence that GPAA1’s luminal domain—despite a protease-like fold—may be more structural/substrate-positioning rather than the main catalytic center (based on mutagenesis and a cell-surface CD59 reporter assay). (xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto pages 7-9)
Accordingly, for S. pombe gaa1/Q9US48, the most conservative functional annotation is: structural/recognition subunit of the ER GPI transamidase complex required for GPI-anchor attachment, likely contributing to substrate recruitment and/or GPI lipid engagement rather than being the protease that cleaves the signal peptide. (vainauskas2002structuralrequirementsfor pages 1-1, vainauskas2004aconservedproline pages 1-1, xu2022molecularinsightsinto pages 7-9)
The GPI transamidase complex catalyzes:
1) cleavage of the precursor’s C-terminal GPI signal peptide at the ω-site, forming an enzyme–substrate intermediate, and
2) nucleophilic attack by GPI to yield a product in which the ω-site residue becomes the C-terminal residue, linked by an amide bond to the GPI ethanolamine/phosphoethanolamine. (vainauskas2004aconservedproline pages 1-1, vainauskas2002structuralrequirementsfor pages 1-1)
Substrate constraints include a preference for small ω-site residues and strong constraints at ω+1/ω+2, plus a hydrophilic spacer and hydrophobic tail downstream. (xu2022molecularinsightsinto pages 2-4, gamage2013gpitransamidaseand pages 3-5, vainauskas2004aconservedproline pages 1-1)
For Gaa1/GPAA1 specifically, experimental and mechanistic studies support roles in substrate recognition and GPI recognition (see above), i.e., it contributes to the complex’s effective substrate processing and lipid engagement rather than defining a classic enzyme-substrate reaction on its own. (vainauskas2002structuralrequirementsfor pages 1-1, vainauskas2004aconservedproline pages 1-1)
Across systems where it has been experimentally studied, Gaa1/GPAA1 is a multi-pass ER membrane glycoprotein. In a detailed mammalian analysis, Gaa1 is ER-localized, with a cytosolic N-terminus and luminal C-terminus, and with a large luminal region important for interactions with other GPI-T subunits. (vainauskas2002structuralrequirementsfor pages 1-1)
A 2022 cryo-EM structure of human GPI-T shows the complex partitioned into a luminal domain and a transmembrane domain, with GPAA1 contributing a substantial portion of the membrane-embedded scaffold (an eight-transmembrane-helix entity in the model). (xu2022molecularinsightsinto pages 2-4)
For S. pombe gaa1/Q9US48, the most defensible localization statement is ER membrane, inferred from conserved complex function and topology across eukaryotes. (vainauskas2002structuralrequirementsfor pages 1-1, xu2022molecularinsightsinto pages 2-4)
The major recent step-change for understanding GPI transamidase is the 2.53 Å cryo-EM structure of the human GPI-T complex, revealing an equimolar heteropentameric organization and providing extensive mutational validation of catalytic and binding determinants. (xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto pages 1-2)
Key quantitative details from this work include: resolution 2.53 Å, near-complete model (2,393 residues, 94.4% complete), and a transmembrane domain comprising 24 TM helices with GPAA1 contributing an eight-TMH module; a ~22 Å elongated cavity spans from the membrane toward the catalytic dyad, supporting a geometry-based model for accommodating both amphipathic protein and lipid substrates. (xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto pages 1-2)
This structure also provided functional assay readouts (e.g., substitutions that abolish activity or reduce to ~10% for a key pocket mutation in the catalytic subunit) and suggested that GPAA1 is less likely to be the principal catalytic site in the human enzyme (based on mutational tolerance in the assay). (xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto pages 7-9)
A 2024 Nature Communications study links ER-associated degradation (ERAD) via the SEL1L–HRD1 complex to GPI-anchored protein biogenesis by identifying PIGK (the catalytic subunit of GPI-T) as a prominent ERAD substrate and showing that ERAD attenuates GPI-anchored protein production by targeting PIGK for proteasomal degradation. (wei2024proteomicscreensof pages 1-2)
Quantitative/statistical highlights from the 2024 work include:
- >100 high-confidence ERAD substrates identified (after machine-learning filtering) across HEK293T cells and mouse brown adipose tissue, with ~88% being cell-type specific. (wei2024proteomicscreensof pages 1-2)
- In one dataset: 55 SEL1L interactors; among putative substrates, 61% membrane proteins, 69% glycosylated, and 31% with disulfide bonds—consistent with surveillance of secretory-pathway proteins and complexes such as GPI-T. (wei2024proteomicscreensof pages 2-3)
While not S. pombe-specific, this work reframes GPI-anchor attachment as a pathway whose throughput can be controlled by protein quality-control systems acting on transamidase subunits; by orthology, similar logic may apply in fungi, although direct evidence would be required for S. pombe. (wei2024proteomicscreensof pages 1-2)
GPI anchoring is central to the cell-surface display of many proteins. For example, the 2024 ERAD study reiterates that there are >150 human GPI-anchored proteins, emphasizing the breadth of pathway impact. (wei2024proteomicscreensof pages 1-2)
In clinical genetics and cell biology, disruptions of GPI transamidase components and GPI biosynthesis are widely connected to human disease; the 2024 work notes that many genetic variants in transamidase components are associated with neurodevelopmental disorders and demonstrates ERAD handling of disease variants in PIGK. (wei2024proteomicscreensof pages 2-3, wei2024proteomicscreensof pages 1-2)
In yeast and fungal systems, GPI anchoring is a major contributor to cell wall protein display and surface proteome composition. Therefore, GPI-transamidase components (including Gaa1 family proteins) are used implicitly in:
- engineered display of proteins on the cell surface (requiring functional GPI attachment machinery), and
- functional genomics screens of secretory pathway/cell wall integrity (GPI anchoring is a frequent node of sensitivity).
Although the accessible corpus here did not provide S. pombe-specific implementations for SPAC1002.11, the conserved essential role of the pathway in anchoring suggests that gaa1 disruption would be expected to broadly affect GPI-anchored protein maturation and downstream cell surface/cell wall processes (hypothesis; would require direct S. pombe validation). (vainauskas2002structuralrequirementsfor pages 1-1, gamage2013gpitransamidaseand pages 3-5)
Older mechanistic syntheses and modeling papers proposed that GAA1/GPAA1 is the key enzymatic subunit catalyzing the peptide-bond formation between the ω-site and phosphoethanolamine and emphasized a metalloenzyme-like luminal domain. (eisenhaber2014transamidasesubunitgaa1gpaa1 pages 4-5, su2020structuralmodellingof pages 1-2)
In contrast, the near-atomic structure and mutagenesis from 2022 provide strong evidence placing proteolytic and transamidation catalysis at the PIGK active site (cysteine protease-like), while supporting GPAA1 as more of a scaffold/substrate-positioning and membrane-embedded organizing unit, with functional importance in building the composite substrate/lipid-binding environment. (xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto pages 7-9)
For functional annotation of S. pombe gaa1/Q9US48, the best practice is therefore to phrase Gaa1’s role as required component of ER GPI transamidase, likely contributing to substrate recruitment and/or GPI recognition, rather than asserting sole catalytic responsibility for peptide-bond formation. (vainauskas2002structuralrequirementsfor pages 1-1, vainauskas2004aconservedproline pages 1-1, xu2022molecularinsightsinto pages 7-9)
The most defensible conserved features (supported by cross-species evidence and conserved complex biology) are:
- ER localization and multi-pass membrane nature of Gaa1-family proteins (vainauskas2002structuralrequirementsfor pages 1-1)
- involvement in GPI recognition/presentation via the last TM segment, including a conserved proline motif (vainauskas2004aconservedproline pages 1-1)
- existence of a S. pombe ortholog in the conserved family bearing the motif (vainauskas2004aconservedproline pages 4-5)
The following table consolidates direct evidence and clearly marks where S. pombe claims are orthology-based.
| Claim/Topic | Organism/System | Key finding | Quantitative details | Evidence type | Citation (include DOI URL and publication date) |
|---|---|---|---|---|---|
| S. pombe gaa1/Q9US48 identity | Schizosaccharomyces pombe (in multispecies alignment) | A Gaa1 ortholog from S. pombe is explicitly included in cross-species alignment of the last TM segment; the family-defining conserved proline linked to GPI recognition is present, supporting that Q9US48/gaa1 belongs to the Gaa1/GPAA1 GPI-transamidase family. | Conserved proline in a GXXP/GXP-like motif in the last TM segment. | Comparative sequence conservation; family inference | Vainauskas & Menon, 2004-02, JBC, DOI: https://doi.org/10.1074/jbc.M312191200 (vainauskas2004aconservedproline pages 4-5) |
| S. pombe gaa1/Q9US48 function (inferred) | S. pombe gaa1 / UniProt Q9US48 | Best-supported annotation is GPI transamidase component Gaa1, involved in attachment of a preassembled GPI anchor to precursor proteins after C-terminal signal processing. Direct S. pombe-specific biochemical evidence was not retrieved, so this is inferred from strong orthology/family conservation. | No direct S. pombe kinetic data retrieved. | Orthology-based functional inference from conserved GPIT subunit family | Conserved-family evidence summarized from Gaa1/GPAA1 studies (vainauskas2002structuralrequirementsfor pages 1-1, vainauskas2004aconservedproline pages 4-5, hong2003humanpiguand pages 9-10) |
| S. pombe gaa1/Q9US48 localization (inferred) | S. pombe gaa1 / eukaryotic Gaa1 family | Likely an ER membrane protein with a large luminal domain, because Gaa1/GPAA1 is ER-localized across experimentally studied systems and functions in the ER-resident GPI transamidase complex. | Human GPAA1/Gaa1 studied as multi-pass membrane glycoprotein; 7 TM spans in 2002 work, 8 TMHs in 2022 cryo-EM model. | Inference from conserved topology and complex localization | Vainauskas et al., 2002-08, JBC, DOI: https://doi.org/10.1074/jbc.M205402200; Xu et al., 2022-05, Nat Commun, DOI: https://doi.org/10.1038/s41467-022-30250-6 (vainauskas2002structuralrequirementsfor pages 1-1, xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto media f6d12197) |
| S. pombe gaa1/Q9US48 complex membership (inferred) | S. pombe gaa1 / eukaryotic GPIT | Likely a core subunit of the five-subunit GPI transamidase (GPIT/GPI-T) with orthologs of PIGK/Gpi8, PIGT/Gpi16, PIGS/Gpi17, and PIGU/Gab1/Cdc91. | Human structure resolved a 1:1:1:1:1 heteropentamer. | Orthology/family inference supported by conserved complex architecture | Ohishi et al., 2000-05, Mol Biol Cell, DOI: https://doi.org/10.1091/mbc.11.5.1523; Xu et al., 2022-05, Nat Commun, DOI: https://doi.org/10.1038/s41467-022-30250-6 (xu2022molecularinsightsinto pages 2-4, hong2003humanpiguand pages 9-10) |
| 2002 structural role of Gaa1 | Human Gaa1 in GPIT | Gaa1 is an ER-localized membrane glycoprotein; its large luminal domain mediates interaction with other GPIT subunits, while C-terminal TM segments are required for a functional complex. | Detergent-extracted Gaa1-containing complexes sedimented at ~17 S. | Primary experimental cell biology and structure-function analysis | Vainauskas et al., 2002-08, JBC, DOI: https://doi.org/10.1074/jbc.M205402200 (vainauskas2002structuralrequirementsfor pages 1-1) |
| 2002 substrate-recognition role | Human Gaa1/GPIT | Pro-protein substrates can bind Gaa1 in the absence of Gpi8, implying a key substrate-recognition/recruitment role for Gaa1 within GPIT. | No catalytic rate reported. | Primary experimental interaction analysis | Vainauskas et al., 2002-08, JBC, DOI: https://doi.org/10.1074/jbc.M205402200 (vainauskas2002structuralrequirementsfor pages 1-1) |
| 2004 GPI recognition by Gaa1 TM segment | Human Gaa1/GPIT with cross-species comparison | A conserved proline in the last TM segment is required for GPI recognition by GPIT; mutant complexes can assemble and bind proprotein yet fail to co-precipitate GPI efficiently. | Example: P609L lost H8/GPI co-precipitation, whereas W611L retained it. | Primary mutational/biochemical evidence | Vainauskas & Menon, 2004-02, JBC, DOI: https://doi.org/10.1074/jbc.M312191200 (vainauskas2004aconservedproline pages 4-5, vainauskas2004aconservedproline pages 5-6) |
| 2022 GPIT architecture | Human GPI transamidase cryo-EM | Near-atomic structure showed an equimolar heteropentameric complex with a luminal catalytic assembly and transmembrane core; GPAA1 forms a major membrane-embedded scaffold with a portico-like architecture. | 2.53 Å resolution; 2,393 residues modeled (94.4% complete); 24 TMHs total; GPAA1 contributes 8 TMHs. | Primary structural biology (cryo-EM) | Xu et al., 2022-05, Nat Commun, DOI: https://doi.org/10.1038/s41467-022-30250-6 (xu2022molecularinsightsinto pages 2-4, xu2022molecularinsightsinto pages 1-2, xu2022molecularinsightsinto media f6d12197) |
| 2022 catalytic assignment revises GPAA1 role | Human GPIT | Structure and mutagenesis support PIGK as the catalytic cysteine protease; GPAA1’s soluble domain resembles a Zn-protease fold but tested acidic/histidine residues were not required in the cell assay, arguing GPAA1 is more likely structural/substrate-positioning rather than the principal catalyst. | GPAA1 D/E/H substitutions did not reduce CD59 staining; PIGK H164A or C206S abolished activity; R60E left 9.8% of WT activity. | Primary structural biology plus mutagenesis | Xu et al., 2022-05, Nat Commun, DOI: https://doi.org/10.1038/s41467-022-30250-6 (xu2022molecularinsightsinto pages 7-9, xu2022molecularinsightsinto pages 2-4) |
| 2022 substrate selectivity model | Human GPIT | The active site forms an elongated cavity spanning from the membrane toward the catalytic dyad, with the distance to the membrane proposed as a molecular ruler for selecting valid GPI-attachment signals. | Cavity extends ~22 Å from membrane toward catalytic dyad; 12/22 mapped pathogenic mutations clustered near catalytic/GPI-binding regions. | Primary structural/mechanistic inference | Xu et al., 2022-05, Nat Commun, DOI: https://doi.org/10.1038/s41467-022-30250-6 (xu2022molecularinsightsinto pages 7-9, xu2022molecularinsightsinto pages 1-2) |
| GAA1/GPAA1 catalytic hypothesis from modeling | Human GPAA1 lumenal domain | Modeling work proposed GPAA1 as an M28-family metallo-peptide synthetase with likely single-Zn chemistry and dynamic flaps around the active site, offering a mechanistic explanation for peptide-bond formation to phosphoethanolamine. | Predicted one Zn favored over two; two flaps show anti-correlated “breathing” dynamics. | Computational structural inference | Su et al., 2020-09, Biology Direct, DOI: https://doi.org/10.1186/s13062-020-00266-3 (su2020structuralmodellingof pages 1-2) |
| ω-site specificity concept | Eukaryotic GAA1/GPAA1 literature | Classical GPAA1-centered model proposes transfer to proteins bearing a GPI-attachment ω-site with limited residue tolerance. | Permissive ω-site residues summarized as Ala, Asn, Asp, Cys, Gly, Ser. | Review/synthesis of prior biochemical literature | Eisenhaber et al., 2014-04, Cell Cycle, DOI: https://doi.org/10.4161/cc.28761 (eisenhaber2014transamidasesubunitgaa1gpaa1 pages 4-5) |
| 2024 ERAD regulation of GPI-T biogenesis | Human HEK293T cells and mouse brown adipose tissue | SEL1L–HRD1 ERAD regulates GPI-anchored protein biogenesis by targeting PIGK for degradation, thereby indirectly controlling the function of the whole GPIT complex containing GPAA1/GAA1. | Screen identified >100 high-confidence endogenous ERAD substrates, with ~88% cell-type specificity. | Primary proteomics and cell biology | Wei et al., 2024-01, Nat Commun, DOI: https://doi.org/10.1038/s41467-024-44948-2 (wei2024proteomicscreensof pages 1-2) |
| 2024 quantitative screen characteristics | Human ERAD interactome | In the SEL1L-centered interactome, many candidate substrates had features common to secretory-pathway proteins, consistent with surveillance of GPI-T/GPI-AP biogenesis. | 55 SEL1L interactors; 61% membrane proteins, 69% glycosylated, 31% with disulfide bonds. | Primary proteomics dataset | Wei et al., 2024-01, Nat Commun, DOI: https://doi.org/10.1038/s41467-024-44948-2 (wei2024proteomicscreensof pages 2-3) |
| 2024 relevance to disease and GPI-AP output | Human GPI-T / ERAD | Several disease-associated PIGK variants are ERAD substrates; because GPIT has five core subunits including GPAA1, this work highlights post-translational quality control as an important regulator of the GPI-anchoring pathway. | Context includes >150 human GPI-anchored proteins. | Primary mechanistic study with disease-variant analysis | Wei et al., 2024-01, Nat Commun, DOI: https://doi.org/10.1038/s41467-024-44948-2 (wei2024proteomicscreensof pages 1-2, wei2024proteomicscreensof pages 2-3) |
Table: This table summarizes what is directly known versus inferred for S. pombe gaa1/Q9US48, then places it in the broader mechanistic context of GAA1/GPAA1 research from landmark 2002, 2004, 2022, and 2024 studies. It is useful for separating species-specific evidence from orthology-based annotation and recent pathway-level advances.
Cropped figure regions from the 2022 cryo-EM study illustrate the location of GPAA1 within the heteropentamer and its multi-pass transmembrane arrangement, supporting claims about how Gaa1-family proteins can act as membrane scaffolds for the transamidase. (xu2022molecularinsightsinto media f6d12197, xu2022molecularinsightsinto media c4bf5218)
References
(vainauskas2004aconservedproline pages 4-5): Saulius Vainauskas and Anant K. Menon. A conserved proline in the last transmembrane segment of gaa1 is required for glycosylphosphatidylinositol (gpi) recognition by gpi transamidase*. Journal of Biological Chemistry, 279:6540-6545, Feb 2004. URL: https://doi.org/10.1074/jbc.m312191200, doi:10.1074/jbc.m312191200. This article has 47 citations and is from a domain leading peer-reviewed journal.
(vainauskas2002structuralrequirementsfor pages 1-1): Saulius Vainauskas, Yusuke Maeda, Henry Kurniawan, Taroh Kinoshita, and Anant K. Menon. Structural requirements for the recruitment of gaa1 into a functional glycosylphosphatidylinositol transamidase complex*. The Journal of Biological Chemistry, 277:30535-30542, Aug 2002. URL: https://doi.org/10.1074/jbc.m205402200, doi:10.1074/jbc.m205402200. This article has 57 citations.
(gamage2013gpitransamidaseand pages 3-5): Dilani G. Gamage and Tamara L. Hendrickson. Gpi transamidase and gpi anchored proteins: oncogenes and biomarkers for cancer. Critical Reviews in Biochemistry and Molecular Biology, 48:446-464, Sep 2013. URL: https://doi.org/10.3109/10409238.2013.831024, doi:10.3109/10409238.2013.831024. This article has 71 citations and is from a peer-reviewed journal.
(vainauskas2004aconservedproline pages 1-1): Saulius Vainauskas and Anant K. Menon. A conserved proline in the last transmembrane segment of gaa1 is required for glycosylphosphatidylinositol (gpi) recognition by gpi transamidase*. Journal of Biological Chemistry, 279:6540-6545, Feb 2004. URL: https://doi.org/10.1074/jbc.m312191200, doi:10.1074/jbc.m312191200. This article has 47 citations and is from a domain leading peer-reviewed journal.
(xu2022molecularinsightsinto pages 2-4): Yidan Xu, Guowen Jia, Tingting Li, Zixuan Zhou, Yitian Luo, Yulin Chao, Juan Bao, Zhaoming Su, Qianhui Qu, and Dianfan Li. Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins. Nature Communications, May 2022. URL: https://doi.org/10.1038/s41467-022-30250-6, doi:10.1038/s41467-022-30250-6. This article has 39 citations and is from a highest quality peer-reviewed journal.
(eisenhaber2014transamidasesubunitgaa1gpaa1 pages 2-4): Birgit Eisenhaber, Stephan Eisenhaber, Toh Yew Kwang, Gerhard Grüber, and Frank Eisenhaber. Transamidase subunit gaa1/gpaa1 is a m28 family metallo-peptide-synthetase that catalyzes the peptide bond formation between the substrate protein’s omega-site and the gpi lipid anchor’s phosphoethanolamine. Cell Cycle, 13:1912-1917, Apr 2014. URL: https://doi.org/10.4161/cc.28761, doi:10.4161/cc.28761. This article has 64 citations and is from a peer-reviewed journal.
(eisenhaber2014transamidasesubunitgaa1gpaa1 pages 4-5): Birgit Eisenhaber, Stephan Eisenhaber, Toh Yew Kwang, Gerhard Grüber, and Frank Eisenhaber. Transamidase subunit gaa1/gpaa1 is a m28 family metallo-peptide-synthetase that catalyzes the peptide bond formation between the substrate protein’s omega-site and the gpi lipid anchor’s phosphoethanolamine. Cell Cycle, 13:1912-1917, Apr 2014. URL: https://doi.org/10.4161/cc.28761, doi:10.4161/cc.28761. This article has 64 citations and is from a peer-reviewed journal.
(xu2022molecularinsightsinto pages 7-9): Yidan Xu, Guowen Jia, Tingting Li, Zixuan Zhou, Yitian Luo, Yulin Chao, Juan Bao, Zhaoming Su, Qianhui Qu, and Dianfan Li. Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins. Nature Communications, May 2022. URL: https://doi.org/10.1038/s41467-022-30250-6, doi:10.1038/s41467-022-30250-6. This article has 39 citations and is from a highest quality peer-reviewed journal.
(xu2022molecularinsightsinto pages 1-2): Yidan Xu, Guowen Jia, Tingting Li, Zixuan Zhou, Yitian Luo, Yulin Chao, Juan Bao, Zhaoming Su, Qianhui Qu, and Dianfan Li. Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins. Nature Communications, May 2022. URL: https://doi.org/10.1038/s41467-022-30250-6, doi:10.1038/s41467-022-30250-6. This article has 39 citations and is from a highest quality peer-reviewed journal.
(wei2024proteomicscreensof pages 1-2): Xiaoqiong Wei, You Lu, Liangguang Leo Lin, Chengxin Zhang, Xinxin Chen, Siwen Wang, Shuangcheng Alivia Wu, Zexin Jason Li, Yujun Quan, Shengyi Sun, and Ling Qi. Proteomic screens of sel1l-hrd1 er-associated degradation substrates reveal its role in glycosylphosphatidylinositol-anchored protein biogenesis. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-024-44948-2, doi:10.1038/s41467-024-44948-2. This article has 26 citations and is from a highest quality peer-reviewed journal.
(wei2024proteomicscreensof pages 2-3): Xiaoqiong Wei, You Lu, Liangguang Leo Lin, Chengxin Zhang, Xinxin Chen, Siwen Wang, Shuangcheng Alivia Wu, Zexin Jason Li, Yujun Quan, Shengyi Sun, and Ling Qi. Proteomic screens of sel1l-hrd1 er-associated degradation substrates reveal its role in glycosylphosphatidylinositol-anchored protein biogenesis. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-024-44948-2, doi:10.1038/s41467-024-44948-2. This article has 26 citations and is from a highest quality peer-reviewed journal.
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