Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0013064
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dc.titleDAAM1 is a formin required for centrosome re-orientation during cell migration
dc.contributor.authorAng S.-F.
dc.contributor.authorZhao Z.-S.
dc.contributor.authorLim L.
dc.contributor.authorManser E.
dc.date.accessioned2019-11-07T08:00:58Z
dc.date.available2019-11-07T08:00:58Z
dc.date.issued2010
dc.identifier.citationAng S.-F., Zhao Z.-S., Lim L., Manser E. (2010). DAAM1 is a formin required for centrosome re-orientation during cell migration. PLoS ONE 5 (9) : e13064. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0013064
dc.identifier.issn19326203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/161806
dc.description.abstractBackground: Disheveled-associated activator of morphogenesis 1 (DAAM1) is a formin acting downstream of Wnt signaling that is important for planar cell polarity. It has been shown to promote proper cell polarization during embryonic development in both Xenopus and Drosophila. Importantly, DAAM1 binds to Disheveled (Dvl) and thus functions downstream of the Frizzled receptors. Little is known of how DAAM1 is localized and functions in mammalian cells. We investigate here how DAAM1 affects migration and polarization of cultured cells and conclude that it plays a key role in centrosome polarity. Methodology/Principal Findings: Using a specific antibody to DAAM1, we find that the protein localizes to the acto-myosin system and co-localizes with ventral myosin IIB-containing actin stress fibers. These fibers are particularly evident in the subnuclear region. An N-terminal region of DAAM1 is responsible for this targeting and the DAAM1(1-440) protein can interact with myosin IIB fibers independently of either F-actin or RhoA binding. We also demonstrate that DAAM1 depletion inhibits Golgi reorientation in wound healing assays. Wound-edge cells exhibit multiple protrusions characteristic of unpolarized cell migration. Finally, in U2OS cells lines stably expressing DAAM1, we observe an enhanced myosin IIB stress fiber network which opposes cell migration. Conclusions/Significance: This work highlights the importance of DAAM1 in processes underlying cell polarity and suggests that it acts in part by affecting the function of acto-myosin IIB system. It also emphasizes the importance of the N-terminal half of DAAM1. DAAM1 depletion strongly blocks centrosomal re-polarization, supporting the concept that DAAM1 signaling cooperates with the established Cdc42 associated polarity complex. These findings are also consistent with the observation that ablation of myosin IIB but not myosin IIA results in polarity defects downstream of Wnt signaling. The structure-function analysis of DAAM1 in cultured cells parallels more complex morphological events in the developing embryo. © 2010 Ang et al.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20191101
dc.subjectdisheveled associated activator of morphogenesis 1 protein
dc.subjectF actin
dc.subjectmyosin IIB
dc.subjectprotein Cdc42
dc.subjectregulator protein
dc.subjectRhoA guanine nucleotide binding protein
dc.subjectunclassified drug
dc.subjectWnt protein
dc.subjectamino terminal sequence
dc.subjectarticle
dc.subjectcell migration
dc.subjectcell polarity
dc.subjectcentrosome
dc.subjectcontrolled study
dc.subjectGolgi complex
dc.subjecthuman
dc.subjecthuman cell
dc.subjecthuman cell culture
dc.subjectprotein depletion
dc.subjectprotein function
dc.subjectprotein localization
dc.subjectprotein protein interaction
dc.subjectprotein targeting
dc.subjectstress fiber
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAmino Acid Motifs
dc.subjectAnimals
dc.subjectCell Movement
dc.subjectCell Polarity
dc.subjectCentrosome
dc.subjectCercopithecus aethiops
dc.subjectCOS Cells
dc.subjectHela Cells
dc.subjectHT29 Cells
dc.subjectHumans
dc.subjectMicrofilament Proteins
dc.subjectNonmuscle Myosin Type IIB
dc.subjectProtein Binding
dc.subjectProtein Transport
dc.subjectrho GTP-Binding Proteins
dc.subjectMammalia
dc.typeArticle
dc.contributor.departmentDEPT OF PHARMACOLOGY
dc.description.doi10.1371/journal.pone.0013064
dc.description.sourcetitlePLoS ONE
dc.description.volume5
dc.description.issue9
dc.description.pagee13064
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