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Article Info.
2003.07.31; 36(4) pp. 354~358

Translocation and Phosphorylation of Calcyclin Binding Protein during Retinoic Acid-induced Neuronal Differentiation of Neuroblastoma SH-SY5Y Cells  


Jing Wu, Xinyu Tan, Xiaozhong Peng, Jiangang Yuan* and Boqin Qiang  


National Laboratory of Medical Molecular Biology, Institute of Basic Medical Science, Chinese Academy of Medical Sciences and Peking Union Medical College, National Human Genome Center, Beijing 100005, China  


For better understanding of functions of the Calcyclin Binding Protein (CacyBP) and exploring its possible roles in neuronal differentiation, the subcellular localization of human CacyBP was examined in retinoic acid(RA)-induced and uninduced neuroblastoma SH-SY5Y cells. Immunostaining indicated that CacyBP was present in the cytoplasm of uninduced SH-SY5Y cells, in which the resting Ca2+ concentration was relatively lower than that of RA-induced cells. After the RA induction, immunostaining was seen in both the nucleus and cytoplasm. In the RA-induced differentiated SH-SY5Y cells, CacyBP was phosphorylated on serine residue(s), while it existed in a dephosphorylated form in normal (uninduced) cells. Thus, the phosphorylation of CacyBP occurs when it is translocated to the nuclear region. The translocation of CacyBP during the RA-induced differentiation of SH-SY5Y cells suggested that this protein might play a role in neuronal differentiation.  


Human CacyBP, Neuroblastoma SH-SY5Y, Phosphorylation, RA-induced differentiation, Translocation