Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.4 extracted from

  • Humtsoe, J.O.; Liu, M.; Malik, A.B.; Wary, K.K.
    Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures (2010), Mol. Cell. Biol., 30, 1593-1606.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.4

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant LPP1, LPP2, and LPP3 cDNAs subcloned into the pLNCX2 retroviral vector directly downstream of the human cytomegalovirus immediate-early promoter. Constructs transfected inot human dermal microvascular endothelial cells. HA-tagged wild-type LPP3 (pLNCX2-HA-WT-hLPP3) stably transfected into HEK-293 cells Homo sapiens
wild-type transfected inot human dermal microvascular endothelial cells Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information in confluent endothelial cells, a fraction of p120-catenin associates and colocalizes with LPP3 at the plasma membrane, via the C-terminal cytoplasmic domain, thereby limiting the ability of LPP3 to stimulate beta-catenin/lymphoid enhancer binding factor 1 signaling Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Synonyms

Synonyms Comment Organism
lipid phosphate phosphatase 3
-
 Mus musculus
lipid phosphate phosphatase 3
-
 Homo sapiens
LPP1
-
 Homo sapiens
LPP2
-
 Homo sapiens
LPP3
-
 Mus musculus
LPP3
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction depletion of LPP3 results in destabilization of beta-catenin, which in turn reduces fibronectin synthesis and deposition, which results in inhibition of endothelial cell migration. Reexpression of beta-catenin but not p120-catenin in LPP3-depleted endothelial cells restores de novo synthesis of fibronectin, which mediates endothelial cell migration and formation of branching point structures. LPP3-RAD mutant, which is defective for integrin binding and a LPP3-PD mutant, which is defective for phosphatase activity stimulate lymphoid enhancer binding factor 1-dependent transcription 3- or 5fold, respectively. The LPP3 mutant that lacks both adhesion and lipid phosphatase domains (hLPP3-RAD+PD) fails to stimulate luciferase activity Homo sapiens
physiological function key role for LPP3 in orchestrating phosphatase and tensin-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling in endothelial cell migration, cell-cell adhesion, and formation of branching point structures. In subconfluent endothelial cells, LPP3 induces expression of fibronectin via beta-catenin/lymphoid enhancer binding factor 1 signaling in a phosphatase and tensin homologue-dependent manner. In confluent endothelial cells, depletion of p120-catenin restores LPP3-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling. In confluent endothelial cells, depletion of p120-catenin restores LPP3-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling. C-terminal domain of LPP3 regulates the expression of p120ctn and VE-cadherin as well as formation of branching point structures. LPP1 and LPP2 have no effect on luciferase (lymphoid enhancer binding factor 1) activity, whereas LPP3 yields an 9fold increase in luciferase activity. LPP1 and LPP2 show no change in basal phosphorylation of beta-catenin Homo sapiens
physiological function LPP3 yields an 8fold increase in luciferase (lymphoid enhancer binding factor 1) activity Mus musculus