Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action.
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.
Zhang
Q X
QX
Department of Biochemistry, Lipid and Lipoprotein Research Group, University of Alberta, 357 Heritage Medical Research Centre, Edmonton, Alberta, Canada T6G 2S2.
Pilquil
C S
CS
Dewald
J
J
Berthiaume
L G
LG
Brindley
D N
DN
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
D008246:Lysophospholipids; D008565:Membrane Proteins; C112948:lipid phosphate phosphatase; D010711:Phosphatidate Phosphatase