TY - JOUR
T1 - Identification of c-Fos as a mitotic phosphoprotein
T2 - Regulation of c-Fos by Aurora-A
AU - Yu, Chang Tze Ricky
AU - Wu, Jiunn Chyi
AU - Liao, Mei Chih
AU - Hsu, Shih Lan
AU - Huang, Chi Ying F.
N1 - Funding Information:
We want to thank Dr. Shih-Tze Chen to provide the Aurora-A inducible clones. This research was supported by grants from the National Health Research Institutes, Department of Health (DOH95-TD-G-111-013), and Taichung Veterans General Hospital (TCVGH-957326D) to C. F. Huang.
PY - 2008/1
Y1 - 2008/1
N2 - The c-Fos has been implicated in the regulation of gene expression under a variety of stimuli. It is known that c-Fos undergoes protein phosphorylation, which may subsequently modulate diverse functions in cells. However, less is known about the role and phosphorylation status of c-Fos during mitosis. Here, we showed that c-Fos exhibited an electrophoretic mobility up-shift as detected by SDS-PAGE during mitosis, which is an indication of protein phosphorylation. Aurora-A, but not Aurora-B or -C, serves as one of the kinases catalyzing the mitotic phosphorylation of c-Fos. The mobility up-shift was partially abolished by introducing siRNA or a catalytically inactive form of Aurora-A. Moreover, ectopic expression of the wild type, but not the catalytically inactive form of Aurora-A resulted in the alteration of c-Fos complex formation, suggesting Aurora-A is engaged in the regulation of c-Fos protein-protein interaction. These findings imply that c-Fos may undergo cell cycle dependent phosphorylation, in which some kinases including Aurora-A play a role in catalyzing the post translational modification of c-Fos.
AB - The c-Fos has been implicated in the regulation of gene expression under a variety of stimuli. It is known that c-Fos undergoes protein phosphorylation, which may subsequently modulate diverse functions in cells. However, less is known about the role and phosphorylation status of c-Fos during mitosis. Here, we showed that c-Fos exhibited an electrophoretic mobility up-shift as detected by SDS-PAGE during mitosis, which is an indication of protein phosphorylation. Aurora-A, but not Aurora-B or -C, serves as one of the kinases catalyzing the mitotic phosphorylation of c-Fos. The mobility up-shift was partially abolished by introducing siRNA or a catalytically inactive form of Aurora-A. Moreover, ectopic expression of the wild type, but not the catalytically inactive form of Aurora-A resulted in the alteration of c-Fos complex formation, suggesting Aurora-A is engaged in the regulation of c-Fos protein-protein interaction. These findings imply that c-Fos may undergo cell cycle dependent phosphorylation, in which some kinases including Aurora-A play a role in catalyzing the post translational modification of c-Fos.
KW - Aurora-A
KW - c-Fos
KW - Mitotic phosphorylation
UR - http://www.scopus.com/inward/record.url?scp=36749087054&partnerID=8YFLogxK
U2 - 10.1007/s11373-007-9209-8
DO - 10.1007/s11373-007-9209-8
M3 - Article
C2 - 17926144
AN - SCOPUS:36749087054
SN - 1021-7770
VL - 15
SP - 79
EP - 87
JO - Journal of Biomedical Science
JF - Journal of Biomedical Science
IS - 1
ER -
