4.5 Article

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

Journal

BIOCHEMICAL JOURNAL
Volume 345, Issue -, Pages 181-184

Publisher

PORTLAND PRESS
DOI: 10.1042/0264-6021:3450181

Keywords

ecto-enzyme; glycosylation; lysophosphatidate; phosphatidate phosphohydrolase

Ask authors/readers for more resources

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

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available