【摘 要】
:
The transcription factor Spl is ubiquitously expressed in different cells and thereby regulates the expression of genes involved in many cellular processes.This study reveals that Spl was phosphorylat
【机 构】
:
Institute of Signal Transduction National Cheng Kung University Taiwan
【出 处】
:
BIT Life Sciences 1st Annual World Cancer Congess-2008(2008中
论文部分内容阅读
The transcription factor Spl is ubiquitously expressed in different cells and thereby regulates the expression of genes involved in many cellular processes.This study reveals that Spl was phosphorylated during the mitotic stage in three epithelial tumor cell lines and one glioma cell line.By using different kinase inhibitors, we found that during mitosis in HeLa cells the c-Jun N-terminal kinase 1 (JNK1) was activated that was then required for the phosphorylation of Spl.In addition, blockade of the Sp 1 phosphorylation via an inhibition of the JNK1 activity in mitosis resulted in the ubiquitination and degradation of Spl.JNK1 phosphorylated Sp 1 at threonine 278/739.The Sp 1 mutated at threonine 278/739 was unstable during mitosis, possessing less transcriptional activity for the 12(S)-lipoxygenase expression, and exhibiting a decreased cell growth rate when compared to wild-type Sp 1 in HeLa cells.
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