Scientists led by Kristina Djinovic-Carugo at the Max F. Perutz Laboratories (MFPL) of the University of Vienna and the Medical University of Vienna have elucidated the molecular structure and regulation of the essential muscle protein ?-actinin. The new findings allow unprecedented insights into the protein’s mode of action and its role in muscle disorders. The findings, made in collaboration with King’s College London (KCL), may lead to improved treatments, and are published in the top-class journal Cell.
The illustration shows a surface representation of the alpha-actinin dimer against a background of muscle sarcomeres viewed under the electron microscope. The sarcomeres display a typical striated pattern, and are connected via joint Z-discs, seen as dark black and grey diagonal stripes.
The research was funded in part by the National Cancer Institute (NCI), (RO1CA169519) and the National Institute of Diabetes & Digestive & Kidney Diseases (NIDDK) at the NIH in Bethesda, Maryland.
Euripedes de Almeida Ribeiro, Nikos Pinotsis, Andrea Ghisleni, Anita Salmazo, Petr V. Konarev, Julius Kostan, Bjoern Sjoeblom, Claudia Schreiner, Anton A. Polyansky, Eirini A. Gkougkoulia, Mark R. Holt, Finn L. Aachmann, Bojan Žagrovi?, Enrica Bordignon, Katharina F. Pirker, Dmitri I. Svergun, Mathias Gautel and Kristina Djinovi?-Carugo: The Structure and Regulation of Human Muscle ?-Actinin. Cell. December 2014. DOI: 10.1016/j.cell.2014.10.056