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Journal of Biochemistry Advance Access published online on June 11, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp089
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

CDK11p58 Phosphorylation of PAK1 Ser174 Promotes DLC2 Binding and Roles on Cell Cycle Progression

Xiangfei kong1, Huachen Gan1, Yuqing Hao1, Chunming Cheng1,2, Jianhai Jiang1, Yi Hong1, Junwu Yang1, Hao Zhu1, Yayun Chi1, Xiaojing Yun1 and Jianxin Gu1,2,3

1Gene Research Center, Key Laboratory of Glycoconjugate Research Ministry of Public Health, Shanghai Medical College of Fudan University, Shanghai 200032, P. R. China
2 Institutes of Biomedical Sciences, Fudan University, Shanghai, P.R. China, 200032

3To whom correspondence should be addressed: Jianxin Gu: Tel.: 86-21-54237704; Fax: 86-21-64164489 Email: Jxgu{at}shmu.edu.cn

Received April 13, 2009; Accepted May 29, 2009


  Abstract

CDK11p58, a CDK11 family Ser/Thr kinase, is a G2/M specific protein and contributed to regulation of cell cycle, transcription and apoptotic signal transduction. Recently, CDK11p58 has been reported to exert important functions in mitotic process, such as the regulation of bipolar spindle formation and sister chomatid cohesion. Here we identified p21 activated kinase 1 (PAK1) as a new CDK11p58 substrate and we mapped a new phosphorylation site of Ser174 on PAK1. By mutagenesis we created PAK1174A and PAK1174E, which mimic the dephosphorylated and phosphorylated form of PAK1, further analysis showed PAK1174E could be recruited to myosin V motor complex through binding to dynein light chain 2 (DLC2). PAK1174E could accelerate the mitosis progression in a nocodazole blocked cell model, while PAK1174A exhibited an opposite role. Our results indicated PAK1 may serve as a downstream effector of CDK11p58 during mitosis progression.

Key Words: CDK11p58, PAK1, phosphorylation, cell cycle, mitosis, myosin V, dynein light chain 2


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