Title : Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway.

Pub. Date : 1999 Mar 2

PMID : 10051603






5 Functional Relationships(s)
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1 A PTEN mutant associated with Cowden"s disease (PTEN;G129E) has protein phosphatase activity yet is defective in dephosphorylating inositol 1,3,4,5-tetrakisphosphate in vitro and fails to arrest cells in G1. inositol-1,3,4,5-tetrakisphosphate phosphatase and tensin homolog Homo sapiens
2 A PTEN mutant associated with Cowden"s disease (PTEN;G129E) has protein phosphatase activity yet is defective in dephosphorylating inositol 1,3,4,5-tetrakisphosphate in vitro and fails to arrest cells in G1. inositol-1,3,4,5-tetrakisphosphate phosphatase and tensin homolog Homo sapiens
3 These data suggest a link between induction of a cell-cycle block by PTEN and its ability to dephosphorylate, in vivo, phosphatidylinositol 3,4,5-trisphosphate. phosphatidylinositol 3,4,5-triphosphate phosphatase and tensin homolog Homo sapiens
4 In keeping with this notion, PTEN can inhibit the phosphatidylinositol 3,4, 5-trisphosphate-dependent Akt kinase, a downstream target of phosphatidylinositol 3-kinase, and constitutively active, but not wild-type, Akt overrides a PTEN G1 arrest. Phosphatidylinositols phosphatase and tensin homolog Homo sapiens
5 In keeping with this notion, PTEN can inhibit the phosphatidylinositol 3,4, 5-trisphosphate-dependent Akt kinase, a downstream target of phosphatidylinositol 3-kinase, and constitutively active, but not wild-type, Akt overrides a PTEN G1 arrest. Phosphatidylinositols phosphatase and tensin homolog Homo sapiens