PMID- 10574991
OWN - NLM
STAT- MEDLINE
DCOM- 20000203
LR  - 20191210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 49
DP  - 1999 Dec 3
TI  - Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring
      phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol.
PG  - 35099-106
AB  - Many cell surface proteins are anchored to the membrane via a
      glycosylphosphatidylinositol (GPI) moiety, which is attached to the C terminus of
      the proteins. The core of the GPI anchor is conserved in all eukaryotes but is
      modified by various side chains. We cloned a mouse phosphatidylinositol
      glycan-class N (Pig-n) gene that encodes a 931amino acid protein expressed in the
      endoplasmic reticulum, which is homologous to yeast Mcd4p. We disrupted the gene 
      in F9 embryonal carcinoma cells. In the Pig-n knockout cells, the first mannose
      in the GPI precursors was not modified by phosphoethanolamine. Nevertheless,
      further biosynthetic steps continued with the addition of the third mannose and
      the terminal phosphoethanolamine. The surface expression of Thy-1 was only
      partially affected, indicating that modification of the first mannose by
      phosphoethanolamine is not essential for attachment of GPI anchors in mammalian
      cells. An inhibitor of GPI biosynthesis, YW3548/BE49385A, inhibited transfer of
      phosphoethanolamine to the first mannose in mammalian cells but only slightly
      affected the surface expression of GPI-anchored proteins. Biosynthesis of GPI in 
      the Pig-n knockout cells was not affected by YW3548/BE49385A, and yeast
      overexpressing MCD4 was highly resistant to YW3548/BE49385A, suggesting that
      Pig-n and Mcd4p are targets of this drug.
FAU - Hong, Y
AU  - Hong Y
AD  - Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka 
      University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan.
FAU - Maeda, Y
AU  - Maeda Y
FAU - Watanabe, R
AU  - Watanabe R
FAU - Ohishi, K
AU  - Ohishi K
FAU - Mishkind, M
AU  - Mishkind M
FAU - Riezman, H
AU  - Riezman H
FAU - Kinoshita, T
AU  - Kinoshita T
LA  - eng
SI  - GENBANK/AB030279
SI  - GENBANK/AB030308
SI  - GENBANK/AB030309
SI  - GENBANK/AB030310
SI  - GENBANK/AB030311
SI  - GENBANK/AB030312
SI  - GENBANK/AB030313
SI  - GENBANK/AB030314
SI  - GENBANK/AB030315
SI  - GENBANK/AB030316
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Ethanolamines)
RN  - 0 (Glycoproteins)
RN  - 0 (Glycosylphosphatidylinositols)
RN  - 0 (Lactones)
RN  - 0 (MCD4 protein, S cerevisiae)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Terpenes)
RN  - 0 (YW 3548)
RN  - 78A2BX7AEU (phosphorylethanolamine)
RN  - EC 2.7.- (Phosphotransferases)
RN  - EC 2.7.- (Pign protein, mouse)
RN  - PHA4727WTP (Mannose)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Cloning, Molecular
MH  - Dose-Response Relationship, Drug
MH  - Ethanolamines/*metabolism
MH  - Flow Cytometry
MH  - *Glycoproteins
MH  - Glycosylation/drug effects
MH  - Glycosylphosphatidylinositols/*metabolism
MH  - Lactones/pharmacology
MH  - Mannose/*metabolism
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Microsomes/metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis
MH  - Phosphotransferases
MH  - Proteins/chemistry/genetics/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Recombination, Genetic
MH  - *Saccharomyces cerevisiae Proteins
MH  - Terpenes/pharmacology
MH  - Transfection
EDAT- 1999/11/27 00:00
MHDA- 1999/11/27 00:01
CRDT- 1999/11/27 00:00
PHST- 1999/11/27 00:00 [pubmed]
PHST- 1999/11/27 00:01 [medline]
PHST- 1999/11/27 00:00 [entrez]
AID - 10.1074/jbc.274.49.35099 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 3;274(49):35099-106. doi: 10.1074/jbc.274.49.35099.