Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.013557
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dc.titleFunctional interactions between phosphatase POPX2 and mDia modulate RhoA pathways
dc.contributor.authorXie, Y
dc.contributor.authorTan, E.-J
dc.contributor.authorWee, S
dc.contributor.authorManser, E
dc.contributor.authorLim, L
dc.contributor.authorKoh, C.-G
dc.date.accessioned2020-10-27T06:56:43Z
dc.date.available2020-10-27T06:56:43Z
dc.date.issued2008
dc.identifier.citationXie, 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
dc.identifier.issn0021-9533
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/181025
dc.description.abstractRho 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.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20201031
dc.subjectphosphatase
dc.subjectphosphatase POPX2
dc.subjectprotein Cdc42
dc.subjectprotein mDia1
dc.subjectRac1 protein
dc.subjectRho guanine nucleotide binding protein
dc.subjectRhoA guanine nucleotide binding protein
dc.subjectserum response factor
dc.subjecttranscription factor
dc.subjectunclassified drug
dc.subjectactin polymerization
dc.subjectarticle
dc.subjectcell adhesion
dc.subjectcell motility
dc.subjectcontrolled study
dc.subjectcytoskeleton
dc.subjecthuman
dc.subjecthuman cell
dc.subjectpriority journal
dc.subjectprotein analysis
dc.subjectprotein binding
dc.subjectprotein function
dc.subjectprotein protein interaction
dc.subjectserum responsive element
dc.subjectstress fiber
dc.subjecttranscription regulation
dc.subjectAnimals
dc.subjectBiological Transport
dc.subjectCarrier Proteins
dc.subjectImmunoprecipitation
dc.subjectMice
dc.subjectModels, Biological
dc.subjectNIH 3T3 Cells
dc.subjectPhosphoprotein Phosphatases
dc.subjectProtein Binding
dc.subjectrhoA GTP-Binding Protein
dc.subjectRNA, Small Interfering
dc.subjectSerum Response Factor
dc.subjectSignal Transduction
dc.subjectStress Fibers
dc.subjectTranscription, Genetic
dc.typeArticle
dc.contributor.departmentDEPT OF PHARMACOLOGY
dc.description.doi10.1242/jcs.013557
dc.description.sourcetitleJournal of Cell Science
dc.description.volume121
dc.description.issue4
dc.description.page514-521
dc.published.statePublished
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