TY - JOUR
T1 - Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction
AU - Butkevich, Eugenia
AU - Bodensiek, Kai
AU - Fakhri, Nikta
AU - Von Roden, Kerstin
AU - Schaap, Iwan A T
AU - Majoul, Irina
AU - Schmidt, Christoph F.
AU - Klopfenstein, Dieter R.
PY - 2015/7/6
Y1 - 2015/7/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84936139967&partnerID=8YFLogxK
U2 - 10.1038/ncomms8523
DO - 10.1038/ncomms8523
M3 - Journal articles
C2 - 26146072
AN - SCOPUS:84936139967
VL - 6
JO - Nature Communications
JF - Nature Communications
M1 - 7523
ER -