The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component
The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component
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DOI:
10.1091/mbc.e05-08-0743
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发表时间:
2005-11-01
影响因子:
3.3
通讯作者:
Kinoshita, T
中科院分区:
文献类型:
--
作者:
Murakami, Y;Siripanyaphinyo, U;Kinoshita, T
Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by an unusually complex GPI-N-acetylglucosaminyltransferase (GPI-GnT) consisting of at least six proteins. Here, we report that human GPI-GnT requires another component, termed PIG-Y, a 71 amino acid protein with two transmembrane domains. The Burkitt lymphoma cell line Daudi, severely defective in the surface expression of GPI-anchored proteins, was a null mutant of PIG-Y. A complex of six components was formed without PIG-Y. PIG-Y appeared to be directly associated with PIG-A, implying that PIG-Y is the key molecule that regulates GPI-GnT activity by binding directly to the catalytic subunit PIG-A. PIG-Y is probably homologous to yeast Eri1p, a component of GPI-GnT. We did not obtain evidence for a functional linkage between GPI-GnT and ras GTPases in mammalian cells as has been reported for yeast cells. A single transcript encoded PIG-Y and, to its 5' side, another protein PreY that has homologues in a wide range of organisms and is characterized by a conserved domain termed DUF343. These two proteins are translated from one mRNA by leaky scanning of the PreY initiation site.