Title : Heat Shock Protein 90 regulates the stability of c-Jun in HEK293 Cells.

Pub. Date : 2007 Oct 31

PMID : 17978573






3 Functional Relationships(s)
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1 We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxy-carbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
2 We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxy-carbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
3 We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxy-carbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens