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Literature summary for 3.1.3.67 extracted from

  • Kini, V.; Chavez, A.; Mehta, D.
    A new role for PTEN in regulating transient receptor potential canonical channel 6-mediated Ca2+ entry, endothelial permeability, and angiogenesis (2010), J. Biol. Chem., 285, 33082-33091.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.67

Activating Compound

Activating Compound Comment Organism Structure
thrombin transiently increases PTEN lipid phosphatase activity by about 2.5fold within 1 min, which remains elevated for 5 min Homo sapiens

Protein Variants

Protein Variants Comment Organism
C124S the PTEN mutant lacks phosphatase activity, but is not altered in TRPC6 activity Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O Homo sapiens
-
 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pulmonary artery endothelial cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
-
 Homo sapiens 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
phosphatase and tensin homologue
-
 Homo sapiens
PTEN
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction thrombin transiently increases PTEN lipid phosphatase activity, while pretreatment of HPAE cells with bpV(pic) slightly reduces basal PTEN activity.Thrombin fails to induce PTEN activity in cells pretreated with bpV(pic). Inhibiting PTEN activity also decreases Akt phosphorylation, inhibiting PTEN phosphatase activity has no effect on thrombin-induced Ca2+ entry Homo sapiens
physiological function phosphatase and tensin homologue is a dual lipidprotein phosphatase that catalyzes the conversion of phosphoinositol 3,4,5-triphosphate to phosphoinositol 4,5-bisphosphate and thereby inhibits PI3K-Akt-dependent cell proliferation, migration, and tumor vascularization. But PTEN is indicated to play a role beyond suppressing PI3K signaling, it also plays a role in regulating Ca2+ entry through transient receptor potential canonical channel 6, TRPC6, that does not require PTEN phosphatase activity, overview. PTEN tail-domain residues 394-403 permit PTEN to associate with TRPC6. The inflammatory mediator thrombin promotes this association. Deletion of PTEN residues 394-403 prevents TRPC6 cell surface expression and Ca2+ entry, regulation, overview Homo sapiens