FEBS Letters | |
PKC‐dependent phosphorylation of the p97 repressor regulates the transcription of aldolase A L‐type promoter | |
Zevino, Chiara1  Izzo, Paola1  Costanzo, Paola1  Medugno, Lina1  Lupo, Angelo1  D'Agostino, Paola1  | |
[1] Dipartimento di Biochimica e Biotecnologie Mediche, Facoltà di Medicina e Chirurgia, Università di Napoli ‘Federico II’, via S. Pansini 5, 80131 Naples, Italy | |
关键词: Negative cis element; Protein kinase C; Phosphorylation; Cell cycle; Transcriptional regulation; CAT; chloramphenicol acetyltransferase; AldA-NRE; aldolase A negative regulatory element; EMSA; electrophoretic mobility shift assay; TPA; phorbol ester 12-O-tetradecanoylphorbol 13-acetate; H7; 1-(5-isoquinolinesulphonyl)-2-methylpiperazine; 4NPP; 4-nitrophenylphosphate; PAP; potato acid phosphatase; | |
DOI : 10.1016/S0014-5793(99)00775-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Expression of mouse aldolase A L-type mRNA is negatively modulated by a cis element (AldA-NRE), located within the aldolase A distal promoter (pL). AldA-NRE interacts with a 97-kDa repressor protein (p97), which binds DNA in a cell cycle-dependent manner. We demonstrate that the binding between AldA-NRE and p97 decreases during differentiation of human Caco-2 cells and is inversely correlated with L-type mRNA expression. Phosphorylation of the p97 repressor weakened its DNA binding activity in differentiated Caco-2 cells, while dephosphorylation enhanced the binding in proliferating cells. Stimulation of protein kinase C (PKC) in vivo decreased the binding of p97 to AldA-NRE and stimulated transcription, while inhibition of PKC stimulated p97 binding and downregulated transcription. These findings suggest that PKC is a mediator of the binding and silencing function of the p97/AldA-NRE repressor complex.
【 授权许可】
Unknown
【 预 览 】
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