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Matches in Nanopublications for { ?s ?p "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" ?g. }

• _5 value "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" provenance.
• _5 value "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" provenance.
• _5 value "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" provenance.
• _5 value "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" provenance.
• _5 value "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" provenance.
• _5 value "insulin also stimulates the transcriptional activity of nSREB2 and nSREB1A through a mitogen activated protein kinase pathway. The ser117 residue has been identified as the major phosphorylation site for MAPK in SREB1A. Ser432 and Ser455 are described as the MAPK phosphorylation sites in viro and in vivo in SREBP2. These phosphorylations do not modify DNA binding but enhance SREBP2 transactivation capacity. A role for MAPK in the modification of SREB1C transcriptional activity remains controversial. Although the ser117 target of MAPK in SREBP1A is also present in the SREBP1C isoform, the use of inhibitors of teh MAPK pathway in cultured hepatocytes do not antagonize the effect of insulin on SREBP1C target genes, suggesting that SREBP1C is not phosphorylated by MAPK in hepatocytes. We have shown that PKB is able to phosphorylate purified nSREBP1C in vitro. Cotransfection experiments in cultured hepatocytes indicate that phosphorylation by insulin and PKB stimulates the transcriptional activity of nuclear SREBP1C" provenance.