Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction
2015 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction
Butkevich, E.; Bodensiek, K.; Fakhri, N.; von Roden, K.; Schaap, I. A. T. ; Majoul, I. & Schmidt, C. et al. (2015)
Nature Communications, 6 art. 7523. DOI: https://doi.org/10.1038/ncomms8523
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- Authors
- Butkevich, Eugenia; Bodensiek, Kai; Fakhri, Nikta; von Roden, Kerstin; Schaap, Iwan A. T. ; Majoul, Irina; Schmidt, Christoph ; Klopfenstein, Dieter R.
- 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 alpha-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 alpha-actinin, tropomyosin and ADF/cofilin and possibly strengthening actin filaments by bundling.
- Issue Date
- 2015
- Publisher
- Nature Publishing Group
- Journal
- Nature Communications
- Organization
- Fakultät für Physik
- ISSN
- 2041-1723