Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action

被引:96
作者
Zhang, QX
Pilquil, CS
Dewald, J
Berthiaume, LG
Brindley, DN
机构
[1] Univ Alberta, Dept Biochem, Signal Transduct Labs, Lipid & Lipoprot Res Grp, Edmonton, AB T6G 2S2, Canada
[2] Univ Alberta, Dept Cell Biol, Lipid & Lipoprot Res Grp, Edmonton, AB T6G 2S2, Canada
关键词
ecto-enzyme; glycosylation; lysophosphatidate; phosphatidate phosphohydrolase;
D O I
10.1042/0264-6021:3450181
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lipid phosphate phosphatase-1 (LPP-1) dephosphorylates exogenous lysophosphatidate and thereby regulates the activation of lysophosphatidate receptors and cell division. Mutation of seven amino acids in three conserved domains of mouse LPP-1 abolished its activity. A glycosylation site was demonstrated between conserved Domains 1 and 2. LPP-1 is expressed in the plasma membrane, and the present results demonstrate the active site to be located on the outer surface.
引用
收藏
页码:181 / 184
页数:4
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