l-683590 and chelerythrine

l-683590 has been researched along with chelerythrine* in 1 studies

Other Studies

1 other study(ies) available for l-683590 and chelerythrine

Article	Year
Signalling pathways regulating the dephosphorylation of Ser729 in the hydrophobic domain of protein kinase Cepsilon upon cell passage. The Journal of biological chemistry, 2001, Mar-30, Volume: 276, Issue:13 We have recently demonstrated that in quiescent fibroblasts protein kinase C (PKC) epsilon(95) is phosphorylated at Ser(729), Ser(703), and Thr(566) and that upon passage of quiescent cells phosphorylation at Ser(729) is lost, giving rise to PKCepsilon(87). Ser(729) may be rephosphorylated later, suggesting cycling between PKCepsilon(87) and PKCepsilon(95). Here we show that the dephosphorylation at Ser(729) is insensitive to okadaic acid, calyculin, ascomycin C, and cyclosporin A, suggesting that dephosphorylation at this site is not mediated through protein phosphatases 1, 2A or 2B. We demonstrate that this dephosphorylation at Ser(729) requires serum and cell readhesion and is sensitive to rapamycin, PD98059, chelerythrine, and Ro-31-8220. These results suggest that the phosphorylation status of Ser(729) in the hydrophobic domain at Ser(729) is regulated independently of the phosphorylation status of other sites in PKCepsilon, by a mTOR-sensitive phosphatase. The mitogen-activated protein kinase pathway and PKC are also implicated in regulating the dephosphorylation at Ser(729). Topics: 3T3 Cells; Alkaloids; Animals; Anti-Bacterial Agents; Benzophenanthridines; Blotting, Western; Calcineurin; Cell Adhesion; Cell Line; Culture Media; Cyclosporine; Down-Regulation; Enzyme Inhibitors; Flavonoids; Indoles; Isoenzymes; MAP Kinase Signaling System; Marine Toxins; Methionine; Mice; Models, Biological; Okadaic Acid; Oxazoles; Phenanthridines; Phosphoprotein Phosphatases; Phosphorylation; Plasmids; Precipitin Tests; Protein Binding; Protein Kinase C; Protein Kinase C-epsilon; Protein Structure, Tertiary; Serine; Signal Transduction; Sirolimus; Tacrolimus; Transfection	2001

Article

Year

Signalling pathways regulating the dephosphorylation of Ser729 in the hydrophobic domain of protein kinase Cepsilon upon cell passage.

The Journal of biological chemistry, 2001, Mar-30, Volume: 276, Issue:13

We have recently demonstrated that in quiescent fibroblasts protein kinase C (PKC) epsilon(95) is phosphorylated at Ser(729), Ser(703), and Thr(566) and that upon passage of quiescent cells phosphorylation at Ser(729) is lost, giving rise to PKCepsilon(87). Ser(729) may be rephosphorylated later, suggesting cycling between PKCepsilon(87) and PKCepsilon(95). Here we show that the dephosphorylation at Ser(729) is insensitive to okadaic acid, calyculin, ascomycin C, and cyclosporin A, suggesting that dephosphorylation at this site is not mediated through protein phosphatases 1, 2A or 2B. We demonstrate that this dephosphorylation at Ser(729) requires serum and cell readhesion and is sensitive to rapamycin, PD98059, chelerythrine, and Ro-31-8220. These results suggest that the phosphorylation status of Ser(729) in the hydrophobic domain at Ser(729) is regulated independently of the phosphorylation status of other sites in PKCepsilon, by a mTOR-sensitive phosphatase. The mitogen-activated protein kinase pathway and PKC are also implicated in regulating the dephosphorylation at Ser(729).

Topics: 3T3 Cells; Alkaloids; Animals; Anti-Bacterial Agents; Benzophenanthridines; Blotting, Western; Calcineurin; Cell Adhesion; Cell Line; Culture Media; Cyclosporine; Down-Regulation; Enzyme Inhibitors; Flavonoids; Indoles; Isoenzymes; MAP Kinase Signaling System; Marine Toxins; Methionine; Mice; Models, Biological; Okadaic Acid; Oxazoles; Phenanthridines; Phosphoprotein Phosphatases; Phosphorylation; Plasmids; Precipitin Tests; Protein Binding; Protein Kinase C; Protein Kinase C-epsilon; Protein Structure, Tertiary; Serine; Signal Transduction; Sirolimus; Tacrolimus; Transfection

2001