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

来源：

BIOCHEMICAL JOURNAL | 2000年 / 345卷

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

页码：181 / 184

页数：4

共 24 条

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