TY - JOUR A1 - Lange, Stephan A1 - Himmel, Mirko A1 - Auerbach, Daniel A1 - Agarkova, Irina A1 - Hayess, Katrin A1 - Fürst, Dieter Oswald A1 - Perriard, Jean-Claude A1 - Ehler, Elisabeth T1 - Dimerisation of myomesin : implications for the structure of the sarcomeric M-band N2 - 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 Y1 - 2005 SN - 0022-2836 ER - TY - JOUR A1 - Wiesner, Sebastian A1 - Salmikangas, Paula A1 - Auerbach, Daniel A1 - Himmel, Mirko A1 - Kempa, Stefan A1 - Hayes, Kathrin A1 - Pacholsky, Dirk A1 - Taivainen, Anu A1 - Schröder, Rolf A1 - Carpen, Olli A1 - Fürst, Dieter Oswald T1 - Indications for a novel muscular dystrophy pathway : gamma-filamin, the muscle-specific filamin isoform, intgeracts with myotilin Y1 - 2000 ER -