PubMed:10051603 JSONTXT

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":41,"end":46},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":156,"end":161},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":282,"end":290},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":300,"end":316},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":397,"end":409},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T7","span":{"begin":411,"end":419},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T8","span":{"begin":425,"end":450},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T9","span":{"begin":558,"end":561},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T10","span":{"begin":726,"end":742},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T11","span":{"begin":1099,"end":1102},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T12","span":{"begin":1320,"end":1325},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0005070"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"0005070"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"0002254"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"0016063"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"0018177"},{"id":"A6","pred":"mondo_id","subj":"T5","obj":"0020690"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"0005105"},{"id":"A8","pred":"mondo_id","subj":"T8","obj":"0005159"},{"id":"A9","pred":"mondo_id","subj":"T9","obj":"0012833"},{"id":"A10","pred":"mondo_id","subj":"T10","obj":"0016063"},{"id":"A11","pred":"mondo_id","subj":"T11","obj":"0012833"},{"id":"A12","pred":"mondo_id","subj":"T12","obj":"0005070"}],"text":"Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway.\nPTEN/MMAC1 is a tumor suppressor gene located on chromosome 10q23. Inherited PTEN/MMAC1 mutations are associated with a cancer predisposition syndrome known as Cowden's disease. Somatic mutation of PTEN has been found in a number of malignancies, including glioblastoma, melanoma, and carcinoma of the prostate and endometrium. The protein product (PTEN) encodes a dual-specificity protein phosphatase and in addition can dephosphorylate certain lipid substrates. Herein, we show that PTEN protein induces a G1 block when reconstituted in PTEN-null cells. 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. 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. 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. Finally, tumor cells lacking PTEN contain high levels of activated Akt, suggesting that PTEN is necessary for the appropriate regulation of the phosphatidylinositol 3-kinase/Akt pathway."}

{"project":"DisGeNET5_variant_disease","denotations":[{"id":"10051603-6#53#58#geners121909218","span":{"begin":749,"end":754},"obj":"geners121909218"},{"id":"10051603-6#30#46#diseaseC0018553","span":{"begin":726,"end":742},"obj":"diseaseC0018553"}],"relations":[{"id":"53#58#geners12190921830#46#diseaseC0018553","pred":"associated_with","subj":"10051603-6#53#58#geners121909218","obj":"10051603-6#30#46#diseaseC0018553"}],"text":"Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway.\nPTEN/MMAC1 is a tumor suppressor gene located on chromosome 10q23. Inherited PTEN/MMAC1 mutations are associated with a cancer predisposition syndrome known as Cowden's disease. Somatic mutation of PTEN has been found in a number of malignancies, including glioblastoma, melanoma, and carcinoma of the prostate and endometrium. The protein product (PTEN) encodes a dual-specificity protein phosphatase and in addition can dephosphorylate certain lipid substrates. Herein, we show that PTEN protein induces a G1 block when reconstituted in PTEN-null cells. 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. 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. 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. Finally, tumor cells lacking PTEN contain high levels of activated Akt, suggesting that PTEN is necessary for the appropriate regulation of the phosphatidylinositol 3-kinase/Akt pathway."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"10051603-2#15#20#gene5728","span":{"begin":222,"end":227},"obj":"gene5728"},{"id":"10051603-2#93#109#diseaseC0018553","span":{"begin":300,"end":316},"obj":"diseaseC0018553"}],"relations":[{"id":"15#20#gene572893#109#diseaseC0018553","pred":"associated_with","subj":"10051603-2#15#20#gene5728","obj":"10051603-2#93#109#diseaseC0018553"}],"text":"Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway.\nPTEN/MMAC1 is a tumor suppressor gene located on chromosome 10q23. Inherited PTEN/MMAC1 mutations are associated with a cancer predisposition syndrome known as Cowden's disease. Somatic mutation of PTEN has been found in a number of malignancies, including glioblastoma, melanoma, and carcinoma of the prostate and endometrium. The protein product (PTEN) encodes a dual-specificity protein phosphatase and in addition can dephosphorylate certain lipid substrates. Herein, we show that PTEN protein induces a G1 block when reconstituted in PTEN-null cells. 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. 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. 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. Finally, tumor cells lacking PTEN contain high levels of activated Akt, suggesting that PTEN is necessary for the appropriate regulation of the phosphatidylinositol 3-kinase/Akt pathway."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":156,"end":161},"obj":"HP_0002664"},{"id":"T2","span":{"begin":260,"end":266},"obj":"HP_0002664"},{"id":"T3","span":{"begin":318,"end":334},"obj":"HP_0001428"},{"id":"T4","span":{"begin":397,"end":409},"obj":"HP_0100843"},{"id":"T5","span":{"begin":411,"end":419},"obj":"HP_0002861"},{"id":"T6","span":{"begin":1320,"end":1325},"obj":"HP_0002664"}],"text":"Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway.\nPTEN/MMAC1 is a tumor suppressor gene located on chromosome 10q23. Inherited PTEN/MMAC1 mutations are associated with a cancer predisposition syndrome known as Cowden's disease. Somatic mutation of PTEN has been found in a number of malignancies, including glioblastoma, melanoma, and carcinoma of the prostate and endometrium. The protein product (PTEN) encodes a dual-specificity protein phosphatase and in addition can dephosphorylate certain lipid substrates. Herein, we show that PTEN protein induces a G1 block when reconstituted in PTEN-null cells. 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. 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. 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. Finally, tumor cells lacking PTEN contain high levels of activated Akt, suggesting that PTEN is necessary for the appropriate regulation of the phosphatidylinositol 3-kinase/Akt pathway."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":222,"end":227},"obj":"gene:5728"},{"id":"T1","span":{"begin":260,"end":266},"obj":"disease:C0006826"},{"id":"T2","span":{"begin":222,"end":227},"obj":"gene:5728"},{"id":"T3","span":{"begin":260,"end":266},"obj":"disease:C1306459"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway.\nPTEN/MMAC1 is a tumor suppressor gene located on chromosome 10q23. Inherited PTEN/MMAC1 mutations are associated with a cancer predisposition syndrome known as Cowden's disease. Somatic mutation of PTEN has been found in a number of malignancies, including glioblastoma, melanoma, and carcinoma of the prostate and endometrium. The protein product (PTEN) encodes a dual-specificity protein phosphatase and in addition can dephosphorylate certain lipid substrates. Herein, we show that PTEN protein induces a G1 block when reconstituted in PTEN-null cells. 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. 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. 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. Finally, tumor cells lacking PTEN contain high levels of activated Akt, suggesting that PTEN is necessary for the appropriate regulation of the phosphatidylinositol 3-kinase/Akt pathway."}