PIGK explained
GPI-anchor transamidase is an enzyme that in humans is encoded by the PIGK gene.[1] [2]
This gene encodes a member of the cysteine protease family C13 that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is a member of the multisubunit enzyme GPI transamidase and is thought to be its enzymatic component. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins.[2]
Interactions
PIGK has been shown to interact with PIGT[3] and GPAA1.[4] [5]
Further reading
- Benghezal M, Benachour A, Rusconi S, etal . Yeast Gpi8p is essential for GPI anchor attachment onto proteins. . EMBO J. . 15 . 23 . 6575–83 . 1997 . 10.1002/j.1460-2075.1996.tb01048.x . 8978684 . 452482 .
- Meyer U, Benghezal M, Imhof I, Conzelmann A . Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins. . Biochemistry . 39 . 12 . 3461–71 . 2000 . 10727241 . 10.1021/bi992186o .
- Ohishi K, Inoue N, Maeda Y, etal . Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. . Mol. Biol. Cell . 11 . 5 . 1523–33 . 2000 . 10793132 . 10.1091/mbc.11.5.1523. 14864 .
- Spurway TD, Dalley JA, High S, Bulleid NJ . Early events in glycosylphosphatidylinositol anchor addition. substrate proteins associate with the transamidase subunit gpi8p. . J. Biol. Chem. . 276 . 19 . 15975–82 . 2001 . 11278620 . 10.1074/jbc.M010128200 . free .
- Ohishi K, Inoue N, Kinoshita T . PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. . EMBO J. . 20 . 15 . 4088–98 . 2001 . 11483512 . 10.1093/emboj/20.15.4088 . 149153 .
- Vainauskas S, Maeda Y, Kurniawan H, etal . Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex. . J. Biol. Chem. . 277 . 34 . 30535–42 . 2002 . 12052837 . 10.1074/jbc.M205402200 . free .
- Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
- Ohishi K, Nagamune K, Maeda Y, Kinoshita T . Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. . J. Biol. Chem. . 278 . 16 . 13959–67 . 2003 . 12582175 . 10.1074/jbc.M300586200 . free .
- Chen R, Anderson V, Hiroi Y, Medof ME . Proprotein interaction with the GPI transamidase. . J. Cell. Biochem. . 88 . 5 . 1025–37 . 2003 . 12616539 . 10.1002/jcb.10439 . 12875152 .
- Hong Y, Ohishi K, Kang JY, etal . Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. . Mol. Biol. Cell . 14 . 5 . 1780–9 . 2004 . 12802054 . 10.1091/mbc.E02-12-0794 . 165076 .
- Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
- Rual JF, Venkatesan K, Hao T, etal . Towards a proteome-scale map of the human protein-protein interaction network. . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . 2005Natur.437.1173R . 4427026 .
- Kimura K, Wakamatsu A, Suzuki Y, etal . Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. . Genome Res. . 16 . 1 . 55–65 . 2006 . 16344560 . 10.1101/gr.4039406 . 1356129 .
- Gregory SG, Barlow KF, McLay KE, etal . The DNA sequence and biological annotation of human chromosome 1. . Nature . 441 . 7091 . 315–21 . 2006 . 16710414 . 10.1038/nature04727 . 2006Natur.441..315G . free .
Notes and References
- Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME . The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase . Proc Natl Acad Sci U S A . 94 . 23 . 12580–5 . December 1997 . 9356492 . 25045 . 10.1073/pnas.94.23.12580 . 1997PNAS...9412580Y . free .
- Web site: Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K.
- Ohishi . Kazuhito . Nagamune Kisaburo . Maeda Yusuke . Kinoshita Taroh . April 2003 . Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge . J. Biol. Chem. . 278 . 16 . 13959–67 . United States. 0021-9258. 12582175 . 10.1074/jbc.M300586200 . free .
- Ohishi . K . Inoue N . Maeda Y . Takeda J . Riezman H . Kinoshita T . May 2000 . Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins . Mol. Biol. Cell . 11 . 5 . 1523–33 . UNITED STATES. 1059-1524. 10793132 . 14864 . 10.1091/mbc.11.5.1523.
- Vainauskas . Saulius . Maeda Yusuke . Kurniawan Henry . Kinoshita Taroh . Menon Anant K . August 2002 . Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex . J. Biol. Chem. . 277 . 34 . 30535–42 . United States. 0021-9258. 12052837 . 10.1074/jbc.M205402200 . free .