Skip Navigation


Journal of Biochemistry Advance Access originally published online on June 11, 2009
Journal of Biochemistry 2009 146(3):417-427; doi:10.1093/jb/mvp089
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
146/3/417    most recent
mvp089v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Kong, X.
Right arrow Articles by Gu, J.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kong, X.
Right arrow Articles by Gu, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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,*

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

*To whom correspondence should be addressed. Tel: +86-21-54237704, Fax: +86-21-64164489, E-mail: 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 chromatid 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, cell cycle, dynein light chain 2, mitosis, myosin V, PAK1, phosphorylation

Abbreviations: DLC1, dynein light chain 1; DLC2, dynein light chain 2; GIT, G-protein-coupled receptor (GPCR)-kinase interacting protein; IRES, internal ribosome entry site; PAK1, p21 activated kinase 1; MTOCs, microtubule organizing centers; PDK1, 3-phosphoinositide-dependent kinase-1; PIX, PAK1-interacting exchange factor; PKA, protein kinase A


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.