@article{VorgerdvanderVenBruchertseiferetal.2005,
  author    = {Vorgerd, M. and vanderVen, Peter F. M. and Bruchertseifer, V. and Lowe, T. and Kley, R. A. and Schr{\"o}der, Rolf and Lochmuller, H. and Himmel, Mirko and Koehler, K. and F{\"u}rst, Dieter Oswald and Huebner, A.},
  title     = {A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy},
  issn      = {0002-9297},
  year      = {2005},
  abstract  = {Myofibrillar myopathy (MFM) is a human disease that is characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. In an extended German pedigree with a novel form of MFM characterized by clinical features of a limb-girdle myopathy and morphological features of MFM, we identified a cosegregating, heterozygous nonsense mutation (8130G -> A; W2710X) in the filamin c gene ( FLNC) on chromosome 7q32.1. The mutation is the first found in FLNC and is localized in the dimerization domain of filamin c. Functional studies showed that, in the truncated mutant protein, this domain has a disturbed secondary structure that leads to the inability to dimerize properly. As a consequence of this malfunction, the muscle fibers of our patients display massive cytoplasmic aggregates containing filamin c and several Z-disk-associated and sarcolemmal proteins},
  language  = {en}
}
@article{BeathamMiddletonRomeroetal.2004,
  author    = {Beatham, Jane L. and Middleton, A. and Romero, Rosario and VanderVen, Peter F. M. and Blanco, Gonzalo},
  title     = {Functional characterisation of the Ky protein},
  issn      = {0960-8966},
  year      = {2004},
  language  = {en}
}
@article{GehmlichGeierOsterzieletal.2004,
  author    = {Gehmlich, Katja and Geier, C. and Osterziel, Karl Joseph and VanderVen, Peter F. M. and F{\"u}rst, Dieter Oswald},
  title     = {Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy},
  issn      = {0302-766X},
  year      = {2004},
  abstract  = {Previous work has shown that mutations in muscle LIM protein (MLP) can cause hypertrophic cardiomyopathy (HCM). In order to gain an insight into the molecular basis of the disease phenotype, we analysed the binding characteristics of wild-type MLP and of the (C58G) mutant MLP that causes hypertrophic cardiomyopathy. We show that MLP can form a ternary complex with two of its previously documented myofibrillar ligand proteins, N-RAP and alpha-actinin, which indicates the presence of distinct, non-overlapping binding sites. Our data also show that, in comparison to wild-type MLP, the capacity of the mutated MLP protein to bind both N-RAP and alpha-actinin is significantly decreased. In addition, this single point mutation prevents zinc coordination and proper folding of the second zinc-finger in the first LIM domain, which consequently renders the protein less stable and more susceptible to proteolysis. The molecular basis for HCM-causing mutations in the MLP gene might therefore be an alteration in the equilibrium of interactions of the ternary complex MLP-N-RAP-alpha-actinin. This assumption is supported by the previous observation that in the pathological situation accompanied by MLP down regulation, cardiomyocytes try to compensate for the decreased stability of MLP protein by increasing the expression of its ligand N-RAP, which might finally result in the development of myocyte disarray that is characteristic of this disease},
  language  = {en}
}
@article{BeathamRomeroTownsendetal.2004,
  author    = {Beatham, Jane L. and Romero, Rosario and Townsend, Stuart K.M. and Hacker, Terry and VanderVen, Peter F. M. and Blanco, Gonzalo},
  title     = {Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres},
  issn      = {0964-6906},
  year      = {2004},
  abstract  = {The KY protein has been implicated in a neuromuscular dystrophy in the mouse, but its role in muscle function remains unclear. Here, we show that KY interacts with several sarcomeric cytoskeletal proteins including, amongst others, filamin C and the slow isoform of the myosin-binding protein C. These interactions were confirmed in vitro and because of its central role in skeletal muscle disease, characterized in more detail for filamin C. A role for KY in regulating filamin C function in vivo is supported by the expression analysis of filamin C in the null ky mouse mutant, where distinct irregular subcellular localization of filamin C was found in subsets of muscle fibres, which appears to be a specific outcome of KY deficiency. Furthermore, KY shows protease activity in in vitro assays, and specific degradation of filamin C by KY is shown in transfected cells. Given the enzymatic nature of the KY protein, it is likely that some of the identified partners are catalytic substrates. These results suggest that KY is an intrinsic part of the protein networks underlying the molecular mechanism of several limb-girdle muscular dystrophies, particularly those where interactions between filamin C and disease causing proteins have been shown},
  language  = {en}
}
@article{PacholskyVakeelHimmeletal.2004,
  author    = {Pacholsky, Dirk and Vakeel, Padmanabhan and Himmel, Mirko and Lowe, T. and Stradal, T. and Rottner, K. and F{\"u}rst, Dieter Oswald and vanderVen, Peter F. M.},
  title     = {Xin repeats define a novel actin-binding motif},
  issn      = {0021-9533},
  year      = {2004},
  abstract  = {Xin is a protein that is expressed during early developmental stages of cardiac and skeletal muscles. Immunolocalization studies indicated a peripheral localization in embryonic mouse heart, where Xin localizes with beta- catenin and N-cadherin. In adult tissues, Xin is found primarily in the intercalated discs of cardiomyocytes and the myotendinous junctions of skeletal muscle cells, both specialized attachment sites of the myofibrillar ends to the sarcolemma. A large part of the Xin protein consists of unique 16 amino acid repeats with unknown function. We have investigated the characteristics of the Xin repeats by transfection experiments and actin-binding assays and ascertained that, upon expression in cultured cells, these repeats bind to and stabilize the actin-based cytoskeleton. In vitro co- sedimentation assays with skeletal muscle actin indicated that they not only directly bind actin filaments, but also have the capability of arranging microfilaments into networks that sediment upon low-speed centrifugation. Very similar repeats were also found in Xin-repeat protein 2' (XIRP2), a novel protein that seems to be expressed mainly in striated muscles. Human XIRP2 contains 28 Xin repeats with properties identical to those of Xin. We conclude that the Xin repeats define a novel, repetitive actin-binding motif present in at least two different muscle proteins. These Xin- repeat proteins therefore constitute the first two members of a novel family of actin-binding proteins},
  language  = {en}
}
@article{HimmelVanderVenStoeckleinetal.2003,
  author    = {Himmel, Mirko and VanderVen, Peter F. M. and St{\"o}cklein, Walter F. M. and F{\"u}rst, Dieter Oswald},
  title     = {The limits of promiscuity : isoform-specific dimerization of filamins},
  year      = {2003},
  language  = {en}
}
@article{VanDerLoopVanDerVenFuerstetal.1996,
  author    = {VanDerLoop, Frank T. L. and VanDerVen, Peter F. M and F{\"u}rst, Dieter Oswald and Gautel, Mathias and VanEys, Guillaume and Ramaekers, Frans C. S.},
  title     = {Integration of titin into the sarcomeres of cultured differentiating human skeletal muscle cells},
  year      = {1996},
  language  = {en}
}
@article{ObermannGautelSteineretal.1996,
  author    = {Obermann, Wolfgang and Gautel, Mathias and Steiner, F. and VanDerVen, Peter F. M. and Weber, Klaus and F{\"u}rst, Dieter Oswald},
  title     = {The structure of the sarcomeric M band : localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy},
  year      = {1996},
  language  = {en}
}
@article{VanDerVenObermannWeberetal.1996,
  author    = {VanDerVen, Peter F. M and Obermann, Wolfgang and Weber, Klaus and F{\"u}rst, Dieter Oswald},
  title     = {Myomesin, M-protein and the structure of the sarcomeric M-band},
  year      = {1996},
  language  = {en}
}
@article{MayansVanDerVenWilmannsetal.1998,
  author    = {Mayans, Olga and VanDerVen, Peter F. M and Wilmanns, Matthias and Mues, Alexander and Young, Paul and F{\"u}rst, Dieter Oswald and Wilmanns, Matthias and Gautel, Mathias},
  title     = {The structural basis of the activation of the serine kinase domain of the giant muscle protein titin during myofibrillogenesis},
  year      = {1998},
  language  = {en}
}