• Login
    Search 
    •   Home
    • Division of Cell and Immune Biology (ZIB)
    • RG Signalling and Motility (SIM)
    • Publications of RG Signalling and Motility (SIM)
    • Search
    •   Home
    • Division of Cell and Immune Biology (ZIB)
    • RG Signalling and Motility (SIM)
    • Publications of RG Signalling and Motility (SIM)
    • Search
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of HZICommunitiesTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)This CollectionTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)

    My Account

    LoginRegister

    Filter by Category

    JournalPLoS computational biology (1)PloS one (1)Authors
    Stradal, Theresia (2)
    Curth, Ute (1)Faix, Jan (1)Gov, Nir S (1)Kabaso, Doron (1)View MoreYear (Issue Date)
    2011 (2)
    TypesArticle (2)

    Local Links

    About: PolicyHelmholtz-Zentrum für Infektionsforschung HomepageHZI-Library HomepageContact usOpen AccessPublishing ApproachGetting StartedEditing ProfileBrowsing OptionsUsing SearchSubmitting Content

    Statistics

    Display statistics
     

    Search

    Show Advanced FiltersHide Advanced Filters

    Filters

    Now showing items 1-2 of 2

    • List view
    • Grid view
    • Sort Options:
    • Relevance
    • Title Asc
    • Title Desc
    • Issue Date Asc
    • Issue Date Desc
    • Results Per Page:
    • 5
    • 10
    • 20
    • 40
    • 60
    • 80
    • 100

    • 2CSV
    • 2RefMan
    • 2EndNote
    • 2BibTex
    • Selective Export
    • Select All
    • Help
    Thumbnail

    Theoretical model for cellular shapes driven by protrusive and adhesive forces.

    Kabaso, Doron; Shlomovitz, Roie; Schloen, Kathrin; Stradal, Theresia; Gov, Nir S (2011-05)
    The forces that arise from the actin cytoskeleton play a crucial role in determining the cell shape. These include protrusive forces due to actin polymerization and adhesion to the external matrix. We present here a theoretical model for the cellular shapes resulting from the feedback between the membrane shape and the forces acting on the membrane, mediated by curvature-sensitive membrane complexes of a convex shape. In previous theoretical studies we have investigated the regimes of linear instability where spontaneous formation of cellular protrusions is initiated. Here we calculate the evolution of a two dimensional cell contour beyond the linear regime and determine the final steady-state shapes arising within the model. We find that shapes driven by adhesion or by actin polymerization (lamellipodia) have very different morphologies, as observed in cells. Furthermore, we find that as the strength of the protrusive forces diminish, the system approaches a stabilization of a periodic pattern of protrusions. This result can provide an explanation for a number of puzzling experimental observations regarding cellular shape dependence on the properties of the extra-cellular matrix.
    Thumbnail

    High-resolution X-ray structure of the trimeric Scar/WAVE-complex precursor Brk1.

    Linkner, Joern; Witte, Gregor; Stradal, Theresia; Curth, Ute; Faix, Jan (2011)
    The Scar/WAVE-complex links upstream Rho-GTPase signaling to the activation of the conserved Arp2/3-complex. Scar/WAVE-induced and Arp2/3-complex-mediated actin nucleation is crucial for actin assembly in protruding lamellipodia to drive cell migration. The heteropentameric Scar/WAVE-complex is composed of Scar/WAVE, Abi, Nap, Pir and a small polypeptide Brk1/HSPC300, and recent work suggested that free Brk1 serves as a homooligomeric precursor in the assembly of this complex. Here we characterized the Brk1 trimer from Dictyostelium by analytical ultracentrifugation and gelfiltration. We show for the first time its dissociation at concentrations in the nanomolar range as well as an exchange of subunits within different DdBrk1 containing complexes. Moreover, we determined the three-dimensional structure of DdBrk1 at 1.5 Å resolution by X-ray crystallography. Three chains of DdBrk1 are associated with each other forming a parallel triple coiled-coil bundle. Notably, this structure is highly similar to the heterotrimeric α-helical bundle of HSPC300/WAVE1/Abi2 within the human Scar/WAVE-complex. This finding, together with the fact that Brk1 is collectively sandwiched by the remaining subunits and also constitutes the main subunit connecting the triple-coil domain of the HSPC300/WAVE1/Abi2/ heterotrimer to Sra1(Pir1), implies a critical function of this subunit in the assembly process of the entire Scar/WAVE-complex.
    DSpace software copyright © 2002-2019  DuraSpace
    Quick Guide | Kontakt | Feedback abschicken
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.