| Structural modelling of the lumenal domain of human GPAA1, the metallo-peptide synthetase subunit of the transamidase complex, reveals zinc-binding mode and two flaps surrounding the active site. | Structural modelling of the lumenal domain of human GPAA1, the metallo-peptide synthetase subunit of the transamidase complex, reveals zinc-binding mode and two flaps surrounding the active site.
Su CT, Sinha S, Eisenhaber B, Eisenhaber F., Free PMC Article | 08/14/2021 |
| Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila. | Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila.
Kawaguchi K, Yamamoto-Hino M, Matsuyama N, Suzuki E, Goto S. | 07/24/2021 |
| GPAA1 promotes progression of childhood acute lymphoblastic leukemia through regulating c-myc. | GPAA1 promotes progression of childhood acute lymphoblastic leukemia through regulating c-myc.
Zhang JX, Wang JH, Sun XG, Hou TZ. | 04/3/2021 |
| A novel variant in GPAA1, encoding a GPI transamidase complex protein, causes inherited vascular anomalies with various phenotypes. | A novel variant in GPAA1, encoding a GPI transamidase complex protein, causes inherited vascular anomalies with various phenotypes.
Li Y, Yang L, Yang J, Shi J, Chai P, Ge S, Wang Y, Fan X, Jia R. | 10/31/2020 |
| Mechanistically, GPAA1 enhanced the levels of metastasis-associated GPI-anchored proteins to increase tumour metastasis and intensified lipid raft formation, which consequently promoted the interaction between EGFR and ERBB2 as well as downstream pro-proliferative signalling. | GPAA1 promotes gastric cancer progression via upregulation of GPI-anchored protein and enhancement of ERBB signalling pathway.
Zhang XX, Ni B, Li Q, Hu LP, Jiang SH, Li RK, Tian GA, Zhu LL, Li J, Zhang XL, Zhang YL, Yang XM, Yang Q, Wang YH, Zhu CC, Zhang ZG., Free PMC Article | 12/21/2019 |
| The splicing mutation was found to decrease GPAA1 mRNA. | Mutations in GPAA1, Encoding a GPI Transamidase Complex Protein, Cause Developmental Delay, Epilepsy, Cerebellar Atrophy, and Osteopenia.
Nguyen TTM, Murakami Y, Sheridan E, Ehresmann S, Rousseau J, St-Denis A, Chai G, Ajeawung NF, Fairbrother L, Reimschisel T, Bateman A, Berry-Kravis E, Xia F, Tardif J, Parry DA, Logan CV, Diggle C, Bennett CP, Hattingh L, Rosenfeld JA, Perry MS, Parker MJ, Le Deist F, Zaki MS, Ignatius E, Isohanni P, Lönnqvist T, Carroll CJ, Johnson CA, Gleeson JG, Kinoshita T, Campeau PM., Free PMC Article | 11/18/2017 |
| the lumenal domain of GAA1/GPAA1 has a 3D structure similar to that of an M28-type aminopeptidase. GAA1/GPAA1 is a candidate for the enzyme that catalyzes the peptide bond formation between the omega-site and a phosphoethanolamine group of GPI lipid anchor. | 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.
Eisenhaber B, Eisenhaber S, Kwang TY, Grüber G, Eisenhaber F., Free PMC Article | 01/24/2015 |
| Results show an increased expression level and elevated copy number for GAA1 in head and neck squamous carcinoma, suggesting a role for this GPI anchor subunit in HNSCC. | Alterations of GPI transamidase subunits in head and neck squamous carcinoma.
Jiang WW, Zahurak M, Zhou ZT, Park HL, Guo ZM, Wu GJ, Sidransky D, Trink B, Califano JA., Free PMC Article | 01/21/2010 |
| Increased expression of glycosyl-phosphatidylinositol anchor attachment protein 1 is associated with gene amplification in hepatocellular carcinoma | Increased expression of glycosyl-phosphatidylinositol anchor attachment protein 1 (GPAA1) is associated with gene amplification in hepatocellular carcinoma.
Ho JC, Cheung ST, Patil M, Chen X, Fan ST. | 01/21/2010 |
| passively retained in the ER by a signalless mechanism | Endoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complex.
Vainauskas S, Menon AK. | 01/21/2010 |
| a conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol recognition by GPI transamidase | A conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol (GPI) recognition by GPI transamidase.
Vainauskas S, Menon AK. | 01/21/2010 |