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Showing 1–7 of 7 results
Advanced filters: Author: Konstantin Kogan Clear advanced filters

  • Depolymerized ADP-actin monomers must be recharged with ATP for new rounds of filament assembly. Here the authors show that cyclase-associated protein (CAP) catalyzes actin nucleotide exchange in vivo and their CAP–actin complex structure reveals the molecular mechanism of CAP-mediated actin nucleotide exchange.

    • Tommi Kotila
    • Konstantin Kogan
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12

  • Focal adhesions are dynamic structures that link the cell to the extracellular matrix. Here, the authors report that focal adhesions contain tropomyosin-decorated actin filaments, and show evidence that suggests specific functions in adhesion dynamics and cell migration.

    • Reena Kumari
    • Katharina Ven
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-20

  • Actin polymerization provides force for vital processes of the eukaryotic cell, but our understanding of actin dynamics and energetics remains limited due to the lack of high-quality probes. Here authors identify a family of highly sensitive fluorescent nucleotide analogues which bind to actin and provide energy to power actin-based processes.

    • Jessica Colombo
    • Adrien Antkowiak
    • Alphée Michelot
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13

  • The cofilin family proteins are actin disassembly factors but the disassembly mechanism is poorly understood. Here authors show that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold and reveal how CAP destabilizes the interface between terminal actin subunits.

    • Tommi Kotila
    • Hugo Wioland
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • The authors report here the structure-function analysis of highly divergent actin from Leishmania parasite. The study reveals remarkably rapid dynamics of parasite actin as well as the underlying molecular basis, thus providing insight into evolution of the actin cytoskeleton.

    • Tommi Kotila
    • Hugo Wioland
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • In this study the authors report that Caldesmon controls force-balance and architecture of stress fibers through dynamic cross-linking of actin and myosin filaments. Caldesmon depletion led to consequent problems in cell morphogenesis, motility and mechanosensing.

    • Shrikant B. Kokate
    • Katarzyna Ciuba
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-20