Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0013064
Title: DAAM1 is a formin required for centrosome re-orientation during cell migration
Authors: Ang S.-F.
Zhao Z.-S.
Lim L.
Manser E. 
Keywords: disheveled associated activator of morphogenesis 1 protein
F actin
myosin IIB
protein Cdc42
regulator protein
RhoA guanine nucleotide binding protein
unclassified drug
Wnt protein
amino terminal sequence
article
cell migration
cell polarity
centrosome
controlled study
Golgi complex
human
human cell
human cell culture
protein depletion
protein function
protein localization
protein protein interaction
protein targeting
stress fiber
Adaptor Proteins, Signal Transducing
Amino Acid Motifs
Animals
Cell Movement
Cell Polarity
Centrosome
Cercopithecus aethiops
COS Cells
Hela Cells
HT29 Cells
Humans
Microfilament Proteins
Nonmuscle Myosin Type IIB
Protein Binding
Protein Transport
rho GTP-Binding Proteins
Mammalia
Issue Date: 2010
Citation: Ang 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
Rights: Attribution 4.0 International
Abstract: Background: 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.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161806
ISSN: 19326203
DOI: 10.1371/journal.pone.0013064
Rights: Attribution 4.0 International
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