The effect of C-terminal fragment of JNK2 on the stability of p53 and cell proliferation.
The basal activity of JNK is low in normal growing cells and inactivated JNK targets p53 for ubiquitination. To elucidate if the C-terminal part of JNK is responsible for its binding to p53, the low background tet-off inducible NIH3T3 cell line was selected by luciferase reporter gene and a double stable C-JNK Aa (203-424) cell line was established. After withdrawing tetracycline, the C-JNK fragment expression was induced and cell growth was dramatically inhibited 24 h later. However, the expression of p53 was found to be increased after the induction of C-JNK fragment, evaluated by transfecting p21waf-luciferase reporter genes. Our further studies showed that C-JNK fragment could form complex with p53 both in vivo and in vitro. Induction of C-JNK fragment in vivo can increase p53 stability by inhibiting p53 ubiquitination.
Yin
Zhi Min
ZM
Jiangsu Province Key Laboratory of Biochemistry and Molecular Biology, College of Life Science, Nanjing Normal University, Nanjing 210097, China. Zhiminy_2000@yahoo.com
Sima
Jian
J
Wu
Yi Fan
YF
Zhu
Jian
J
Jiang
Yong
Y
D016475:3T3 Cells; D000818:Animals; D002460:Cell Line; D049109:Cell Proliferation / Q000187:drug effects*; D051379:Mice; D048056:Mitogen-Activated Protein Kinase 9 / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000494:pharmacology*; D013997:Time Factors; D016159:Tumor Suppressor Protein p53 / Q000187:drug effects* / Q000378:metabolism
D010446:Peptide Fragments; D016159:Tumor Suppressor Protein p53; D048056:Mitogen-Activated Protein Kinase 9