spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 29 January 2008
doi: 10.1242/jcs.013557


Journal of Cell Science 121, 514-521 (2008)
Published by The Company of Biologists 2008
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.013557v1
121/4/514    most recent
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Xie, Y.
Right arrow Articles by Koh, C.-G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Xie, Y.
Right arrow Articles by Koh, C.-G.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research Article

Functional interactions between phosphatase POPX2 and mDia modulate RhoA pathways

Yi Xie1, E-Jean Tan2, Shimei Wee2, Edward Manser2, Louis Lim2,3 and Cheng-Gee Koh1,*

1 School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Republic of Singapore
2 GSK/IMCB Group, Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, Singapore 138673, Republic of Singapore
3 Department of Molecular Neuroscience, Institute of Neurology, University College London, 1 Wakefield Street, London, WC1N 1PJ, UK

* Author for correspondence (e-mail: CGKOH{at}ntu.edu.sg)

Accepted 19 November 2007

Rho GTPases and their downstream effectors regulate changes in the actin cytoskeleton that underlie cell motility and adhesion. They also participate, with RhoA, in the regulation of gene transcription by activating serum response factor (SRF)-mediated transcription from the serum response element (SRE). SRF-mediated transcription is also promoted by several proteins that regulate the polymerization or stability of actin. We have previously identified a family of PP2C phosphatases, POPXs, which can dephosphorylate the CDC42/RAC-activated kinase PAK and downregulate its enzymatic and actin cytoskeletal activity. We now report that POPX2 interacts with the formin protein mDia1 (DIAPH1). This interaction is enhanced when mDia1 is activated by RhoA. The binding of POPX2 to mDia1 or to an mDia-containing complex greatly decreases the ability of mDia1 to activate transcription from the SRE. We propose that the interaction between mDia1 and POPX2 (PPM1F) serves to regulate both the actin cytoskeleton and SRF-mediated transcription, and to link the CDC42/RAC1 pathways with those of RhoA.

Key words: Rho GTPases, POPX phosphatase, Diaphanous-related formin (mDia), Serum response factor (SRF), Actin stress fibres


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
DevelopmentHome page
Y. Xie, E-J. Tan, S. Wee, E. Manser, L. Lim, and C.-G. Koh
Functional interactions between POPX2 phosphatase and mDia modulate RhoA pathways
Development, March 1, 2008; 135(5): e1 - e1.
[Full Text]




© The Company of Biologists Ltd 2008