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Berlin 2015 – scientific programme

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BP: Fachverband Biologische Physik

BP 22: Posters: Cytoskeletal filaments

BP 22.8: Poster

Tuesday, March 17, 2015, 14:00–16:00, Poster A

Drebrin-like protein (DBN-1) is a novel sarcomere component which stabilizes actin filaments during muscle contractionEugenia Butkevich1, Kai Bodensiek1, Nikta Fakhri1, Kerstin von Roden1, Iwan T. Schaap1, 2, Irina Majoul3, Christoph F. Schmidt1, and •Dieter R. Klopfenstein11Drittes Physikalisches Institut, Georg-August-Universität, Friedrich-Hund-Platz 1, 37077 Göttingen — 2Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Göttingen — 3Institute of Biology, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck - Germany

Actin filament organization and stability in the sarcomeres of muscle cells are critical for force generation. Here, we have identified and functionally characterized a C. elegans drebrin-like protein DBN-1 as a crucial constituent of the muscle-contraction machinery in the nematode. In vitro, DBN-1 exhibited actin filament binding and bundling activity. High-resolution AFM showed single DBN-1 molecules decorating the sides of actin filaments. In vivo, DBN-1 is expressed in body wall muscles constituting an essential sarcomere component. Surprisingly, during muscle contraction, DBN-1 alternated location between myosin- and actin-rich regions of the myofilament lattice likely regulating proper spacing of alpha-actinin and tropomyosin. A loss-of-function mutation in dbn-1 resulted in the partial depolymerization of F-actin upon muscle contraction. Taken together, DBN-1 organizes the muscle contractile apparatus maintaining the spatial relationship between actin-binding proteins and strengthening actin filaments by bundling.

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