LNCaP公司
激酶
磷酸酶
生物
c-jun公司
MAPK/ERK通路
分子生物学
丝裂原活化蛋白激酶
磷酸化
细胞生物学
转录因子
生物化学
癌细胞
遗传学
癌症
基因
作者
Jorge Inostroza,Leonardo Sáenz,Gloria M. Calaf,Gertrudis Cabello,Eduardo Parra
标识
DOI:10.4067/s0716-97602005000200006
摘要
The specific signaling connections between the mitogen-activated protein kinases (MAPK) such as c-Jun Nterminal kinase (JNK-1) and phosphatases PP4 and M3/6, affecting the family of early nuclear factors, is complex and remains poorly understood.JNK-1 regulates cellular differentiation, apoptosis and stress responsiveness by up-regulating early nuclear factors such as c-Jun, a member of the activating protein (AP-1) family, and the Early Growth Factor (EGR-1).C-Jun, when phosphorylated by c-Jun N-terminal kinase (JNK-1) associates with c-Fos to form the AP-1 transcription factor that activates gene expression.We have investigated the regulation of the JNK-1 kinase by co-transfecting phosphatases PP4 and M3/6 in prostate cancer cell lines PC-3 and LNCaP, which have been previously stimulated with human EGF or cisplatin.Cotransfections of plasmids expressing the JNK-1 and the serine/threonine phosphatases PP4 resulted in a significant increase in JNK-1 activity in both PC3 and LNCaP cells.In contrast, co-transfection of JNK-1 with the dual specific phosphatase serine/threonine M3/6 showed only a marginal effect in JNK-1 activity.The phosphatase M3/6 also failed in blocking the induction of JNK-1 activity observed in presence of PP4.The higher activity of JNK-1 was associated with increased activities of the factors c-Jun/AP-1 and EGR-1.This suggests that JNK-1 activity in PC-3 and LNCaP cells requires not only active PP4 for stable maintenance but also suggests that the relative degree of phosphorylation of multiple cellular components is the determinant of JNK-1 stability.
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