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 demonstra...

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Bibliographic Details
Published in:Biochemical journal 2000-01, Vol.345 Pt 2 (2), p.181-184
Main Authors: Zhang, Q X, Pilquil, C S, Dewald, J, Berthiaume, L G, Brindley, D N
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Catalytic Domain
Cell Membrane - enzymology
Cells, Cultured
Conserved Sequence
Fibroblasts - cytology
Glycosylation
Lysophospholipids - metabolism
Membrane Proteins
Mice
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Phosphatidate Phosphatase - genetics
Phosphatidate Phosphatase - metabolism
Precipitin Tests
Protein Processing, Post-Translational
Rats
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Description
Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/0264-6021:3450181