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Sunil Nagpal - One of the best experts on this subject based on the ideXlab platform.
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ligand modulates vdr ser thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell context dependent manner
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
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Ligand modulates VDR-Ser/Thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell-context-dependent manner.
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
David J Bettoun - One of the best experts on this subject based on the ideXlab platform.
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ligand modulates vdr ser thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell context dependent manner
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
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Ligand modulates VDR-Ser/Thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell-context-dependent manner.
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
Berket Khalifa - One of the best experts on this subject based on the ideXlab platform.
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ligand modulates vdr ser thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell context dependent manner
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
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Ligand modulates VDR-Ser/Thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell-context-dependent manner.
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
Jianfen Lu - One of the best experts on this subject based on the ideXlab platform.
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ligand modulates vdr ser thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell context dependent manner
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
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Ligand modulates VDR-Ser/Thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell-context-dependent manner.
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
William W Chin - One of the best experts on this subject based on the ideXlab platform.
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ligand modulates vdr ser thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell context dependent manner
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
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Ligand modulates VDR-Ser/Thr protein phosphatase interaction and P70S6 Kinase phosphorylation in a cell-context-dependent manner.
The Journal of Steroid Biochemistry and Molecular Biology, 2004Co-Authors: David J Bettoun, Jianfen Lu, Berket Khalifa, William W Chin, Sunil NagpalAbstract:Abstract We have recently shown that in colon cancer cells, Vitamin D receptor (VDR) interacts with the catalytic subunit of Ser/Thr protein phosphatases, PP1c and PP2Ac, and induces their enzymatic activity in a ligand-dependent manner. The VDR–PP1c and VDR–PP2Ac interactions were ligand independent in vivo, and 1,25-dihydroxyvitamin D 3 (1,25(OH) 2 D 3 )-mediated increase in VDR-associated phosphatase activity resulted in dephosphorylation and inactivation of P70S6 Kinase in colon cancer cells. Here, we demonstrate that in myeloid leukemia cells, 1,25(OH) 2 D 3 treatment increased the Thr389 phosphorylation of P70S6 Kinase. Accordingly, 1,25(OH) 2 D 3 decreased VDR-associated Ser/Thr protein phosphatase activity by dissociating VDR–PP1c and VDR–PP2Ac interactions. Further, 1,25(OH) 2 D 3 increased the association between VDR and Thr389 phosphorylated P70S6 Kinase. Finally, by using non-secosteroidal VDR ligands, we demonstrate a separation between transactivation and P70S6 Kinase phosphorylation activities of VDR and show pharmacologically that P70S6 Kinase phosphorylation correlates with HL-60 cell differentiation.
