Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction

Eugenia Butkevich, Kai Bodensiek, Nikta Fakhri, Kerstin von Roden, Iwan A. T. Schaap, Irina Majoul, Christoph F. Schmidt () and Dieter R. Klopfenstein ()
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Eugenia Butkevich: Drittes Physikalisches Institut, Georg-August-Universität
Kai Bodensiek: Drittes Physikalisches Institut, Georg-August-Universität
Nikta Fakhri: Drittes Physikalisches Institut, Georg-August-Universität
Kerstin von Roden: Drittes Physikalisches Institut, Georg-August-Universität
Iwan A. T. Schaap: Drittes Physikalisches Institut, Georg-August-Universität
Irina Majoul: Institute of Biology, Center for Structural and Cell Biology in Medicine, University of Lübeck
Christoph F. Schmidt: Drittes Physikalisches Institut, Georg-August-Universität
Dieter R. Klopfenstein: Drittes Physikalisches Institut, Georg-August-Universität

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract Actin filament organization and stability in the sarcomeres of muscle cells are critical for force generation. Here we identify and functionally characterize a Caenorhabditis elegans drebrin-like protein DBN-1 as a novel constituent of the muscle contraction machinery. In vitro, DBN-1 exhibits actin filament binding and bundling activity. In vivo, DBN-1 is expressed in body wall muscles of C. elegans. During the muscle contraction cycle, DBN-1 alternates location between myosin- and actin-rich regions of the sarcomere. In contracted muscle, DBN-1 is accumulated at I-bands where it likely regulates proper spacing of α-actinin and tropomyosin and protects actin filaments from the interaction with ADF/cofilin. DBN-1 loss of function results in the partial depolymerization of F-actin during muscle contraction. Taken together, our data show that DBN-1 organizes the muscle contractile apparatus maintaining the spatial relationship between actin-binding proteins such as α-actinin, tropomyosin and ADF/cofilin and possibly strengthening actin filaments by bundling.

Date: 2015
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DOI: 10.1038/ncomms8523

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