title: Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action.
abstract: 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.
authors.affiliation: Department of Biochemistry, Lipid and Lipoprotein Research Group, University of Alberta, 357 Heritage Medical Research Centre, Edmonton, Alberta, Canada T6G 2S2.
authors.forename: Q X
authors.initials: QX
authors.lastname: Zhang
authors.forename: C S
authors.initials: CS
authors.lastname: Pilquil
authors.forename: J
authors.initials: J
authors.lastname: Dewald
authors.forename: L G
authors.initials: LG
authors.lastname: Berthiaume
authors.forename: D N
authors.initials: DN
authors.lastname: Brindley
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D017124:Conserved Sequence; D005347:Fibroblasts / Q000166:cytology; D006031:Glycosylation; D008246:Lysophospholipids / Q000378:metabolism*; D008565:Membrane Proteins; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010711:Phosphatidate Phosphatase / Q000235:genetics / Q000378:metabolism*; D011233:Precipitin Tests; D011499:Protein Processing, Post-Translational; D051381:Rats
chemical_list: D008246:Lysophospholipids; D008565:Membrane Proteins; C112948:lipid phosphate phosphatase; D010711:Phosphatidate Phosphatase