Identification of extracellular signal-regulated kinase 3 as a new interaction partner of cyclin D3.
Cyclin D3, like cyclin D1 and D2 isoforms, is a crucial component of the core cell cycle machinery in mammalian cells. It also exhibits its unique properties in many other physiological processes. In the present study, using yeast two-hybrid screening, we identified ERK3, an atypical mitogen-activated protein kinase (MAPK), as a cyclin D3 binding partner. GST pull-down assays showed that cyclin D3 interacts directly and specifically with ERK3 in vitro. The binding of cyclin D3 and ERK3 was further confirmed in vivo by co-immunoprecipitation assay and confocal microscopic analysis. Moreover, carboxy-terminal extension of ERK3 was responsible for its association with intact cyclin D3. These findings further expand distinct roles of cyclin D3 and suggest the potential activity of ERK3 in cell proliferation.
Sun
Maoyun
M
State Key Laboratory of Genetic Engineering and Gene Research Center, Shanghai Medical College of Fudan University, Shanghai 200032, PR China.
Wei
Yuanyan
Y
Yao
Luyang
L
Xie
Jianhui
J
Chen
Xiaoning
X
Wang
Hanzhou
H
Jiang
Jianhai
J
Gu
Jianxin
J
D001665:Binding Sites; D056743:Cyclin D3; D016213:Cyclins / Q000378:metabolism*; D006801:Humans; D048053:Mitogen-Activated Protein Kinase 6 / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D020798:Two-Hybrid System Techniques
C534696:CCND3 protein, human; D056743:Cyclin D3; D016213:Cyclins; D048053:Mitogen-Activated Protein Kinase 6