@article{LangeHimmelAuerbachetal.2005,
  author    = {Lange, Stephan and Himmel, Mirko and Auerbach, Daniel and Agarkova, Irina and Hayess, Katrin and F{\"u}rst, Dieter Oswald and Perriard, Jean-Claude and Ehler, Elisabeth},
  title     = {Dimerisation of myomesin : implications for the structure of the sarcomeric M-band},
  issn      = {0022-2836},
  year      = {2005},
  abstract  = {The sarcomeric M-band is thought to provide a link between the thick and the elastic, filament systems. So far, relatively little is known about its structural components and their three-dimensional organisation. Myomesin seems to be an essential component of the M-band, since it is expressed in all types of vertebrate striated muscle fibres investigated and can be found in its mature localisation pattern as soon as the first myofibrils are assembled. Previous work has shown that the N-terminal and central part of myomesin harbour binding sites for myosin, titin and muscle creatine kinase. Intrigued by the highly conserved domain layout of the C-terminal half, we screened for new interaction partners by yeast two-hybrid analysis. This revealed a strong interaction of myomesin with itself. This finding was confirmed by several biochemical assays. Our data suggest that myomesin can form antiparallel dimers via a binding site residing in its C-terminal domain 13. We suggest that, similar to alpha-actinin in the Z-disc, the myomesin dimers cross- link the contractile filaments in the M-band. The new and the already previously identified myomesin interaction sites are integrated into the first three-dimensional model of the sarcomeric M-band on a molecular basis. (C) 2004 Elsevier Ltd. All rights reserved},
  language  = {en}
}
@article{GehmlichHayessLegleretal.2010,
  author    = {Gehmlich, Katja and Hayess, Katrin and Legler, Christof and Haebel, Sophie and van der Ven, Peter F. M. and Ehler, Elisabeth and Fuerst, Dieter O.},
  title     = {Ponsin interacts with Nck adapter proteins : implications for a role in cytoskeletal remodelling during differentiation of skeletal muscle cells},
  issn      = {0171-9335},
  doi       = {10.1016/j.ejcb.2009.10.019},
  year      = {2010},
  abstract  = {Skeletal muscle differentiation is a complex process: It is characterised by changes in gene expression and protein composition. Simultaneously, a dramatic remodelling of the cytoskeleton and associated cell-matrix contacts, the costameres, occurs. The expression and localisation of the protein ponsin at cell-matrix contacts marks the establishment of costameres. In this report we show that skeletal muscle cells are characterised by a novel ponsin isoform, which contains a large insertion in its carboxy-terminus. This skeletal muscle-specific module binds the adapter proteins Nck1 and Nck2, and increased co-localisation of ponsin with Nck2 is observed at remodelling cell-matrix contacts of differentiating skeletal muscle cells. Since this ponsin insertion can be phosphorylated, it may adjust the interaction affinity with Nck adapter proteins. The novel ponsin isoform and its interaction with Nck1/2 provide exciting insight into the convergence of signalling pathways at the costameres, and its crucial role for skeletal muscle differentiation and re-generation.},
  language  = {en}
}
@article{VanDerVenEhlerPerriardetal.1999,
  author    = {VanDerVen, Peter and Ehler, Elisabeth and Perriard, Jean-Claude and F{\"u}rst, Dieter Oswald},
  title     = {Thick filament assembly occurs after the formation of a cytoskeletal scaffold.},
  year      = {1999},
  language  = {en}
}
@article{VanderVenEhlerVakeeletal.2006,
  author    = {VanderVen, Peter F. M. and Ehler, Elisabeth and Vakeel, Padmanabhan and Eulitz, Stefan and Schenk, J{\"o}rg A. and Milting, Hendrik and Micheel, Burkhard and F{\"u}rst, Dieter Oswald},
  title     = {Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/ VASP},
  doi       = {10.1016/j.yexcr.2006.03.015},
  year      = {2006},
  abstract  = {Filamin c is the predominantly expressed filamin isoform in striated muscles. It is localized in myofibrillar Z- discs, where it binds FATZ and myotilin, and in myotendinous junctions and intercalated discs. Here, we identify Xin, the protein encoded by the human gene 'cardiomyopathy associated 1' (CMYA1) as filamin c binding partner at these specialized structures where the ends of myofibrils are attached to the sarcolemma. Xin directly binds the EVH1 domain proteins Mena and VASP. In the adult heart, Xin and Mena/VASP colocalize with filamin c in intercalated discs. In cultured cardiomyocytes, the proteins also localize in the nonstriated part of myofibrils, where sarcomeres are assembled and an extensive reorganization of the actin cytoskeleton occurs. Unusual intraexonic splicing events result in the existence of three Xin isoforms that associate differentially with its ligands. The identification of the complex filamin c-Xin-Mena/VASP provides a first glance on the role of Xin in the molecular mechanisms involved in developmental and adaptive remodeling of the actin cytoskeleton during cardiac morphogenesis and sarcomere assembly. (c) 2006 Elsevier Inc. All rights reserved},
  language  = {en}
}