Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.013557
Title: Functional interactions between phosphatase POPX2 and mDia modulate RhoA pathways
Authors: Xie, Y
Tan, E.-J
Wee, S
Manser, E 
Lim, L
Koh, C.-G
Keywords: phosphatase
phosphatase POPX2
protein Cdc42
protein mDia1
Rac1 protein
Rho guanine nucleotide binding protein
RhoA guanine nucleotide binding protein
serum response factor
transcription factor
unclassified drug
actin polymerization
article
cell adhesion
cell motility
controlled study
cytoskeleton
human
human cell
priority journal
protein analysis
protein binding
protein function
protein protein interaction
serum responsive element
stress fiber
transcription regulation
Animals
Biological Transport
Carrier Proteins
Immunoprecipitation
Mice
Models, Biological
NIH 3T3 Cells
Phosphoprotein Phosphatases
Protein Binding
rhoA GTP-Binding Protein
RNA, Small Interfering
Serum Response Factor
Signal Transduction
Stress Fibers
Transcription, Genetic
Issue Date: 2008
Citation: Xie, Y, Tan, E.-J, Wee, S, Manser, E, Lim, L, Koh, C.-G (2008). Functional interactions between phosphatase POPX2 and mDia modulate RhoA pathways. Journal of Cell Science 121 (4) : 514-521. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.013557
Rights: Attribution 4.0 International
Abstract: 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 mDial (DIAPH1). This interaction is enhanced when mDial is activated by RhoA. The binding of POPX2 to mDial or to an mDia-containing complex greatly decreases the ability of mDial to activate transcription from the SRE. We propose that the interaction between mDial 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.
Source Title: Journal of Cell Science
URI: https://scholarbank.nus.edu.sg/handle/10635/181025
ISSN: 0021-9533
DOI: 10.1242/jcs.013557
Rights: Attribution 4.0 International
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