4.5 Article

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

期刊

BIOCHEMICAL JOURNAL
卷 345, 期 -, 页码 181-184

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PORTLAND PRESS
DOI: 10.1042/0264-6021:3450181

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ecto-enzyme; glycosylation; lysophosphatidate; phosphatidate phosphohydrolase

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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.

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