@article {36602,
	title = {The structure and regulation of human muscle alpha-actinin},
	journal = {Cell},
	volume = {159},
	number = {6},
	year = {2014},
	note = {Ribeiro, Euripedes de Almeida JrPinotsis, NikosGhisleni, AndreaSalmazo, AnitaKonarev, Petr VKostan, JuliusSjoblom, BjornSchreiner, ClaudiaPolyansky, Anton AGkougkoulia, Eirini AHolt, Mark RAachmann, Finn LZagrovic, BojanBordignon, EnricaPirker, Katharina FSvergun, Dmitri IGautel, MathiasDjinovic-Carugo, KristinaengI 1593/FWF_/Austrian Science Fund FWF/Austria279408/ERC_/European Research Council/InternationalCH/08/001/BHF_/British Heart Foundation/United KingdomMR/J010456/1/MRC_/Medical Research Council/United KingdomG0200496/MRC_/Medical Research Council/United KingdomMR/K015664/1/MRC_/Medical Research Council/United KingdomI 525/FWF_/Austrian Science Fund FWF/AustriaG0600251/MRC_/Medical Research Council/United KingdomResearch Support, Non-U.S. Gov{\textquoteright}tCell. 2014 Dec 4;159(6):1447-60. doi: 10.1016/j.cell.2014.10.056. Epub 2014 Nov 26.},
	month = {Dec 4},
	pages = {1447-60},
	edition = {2014/12/01},
	abstract = {The spectrin superfamily of proteins plays key roles in assembling the actin cytoskeleton in various cell types, crosslinks actin filaments, and acts as scaffolds for the assembly of large protein complexes involved in structural integrity and mechanosensation, as well as cell signaling. alpha-actinins in particular are the major actin crosslinkers in muscle Z-disks, focal adhesions, and actin stress fibers. We report a complete high-resolution structure of the 200 kDa alpha-actinin-2 dimer from striated muscle and explore its functional implications on the biochemical and cellular level. The structure provides insight into the phosphoinositide-based mechanism controlling its interaction with sarcomeric proteins such as titin, lays a foundation for studying the impact of pathogenic mutations at molecular resolution, and is likely to be broadly relevant for the regulation of spectrin-like proteins.},
	keywords = {Actinin/*chemistry, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Humans, Ligands, Models, Molecular, Molecular Sequence Data, Muscle, Skeletal/chemistry, Protein Structure, Tertiary, Scattering, Small Angle, Sequence Alignment, X-Ray Diffraction},
	isbn = {1097-4172 (Electronic)0092-8674 (Print)0092-8674 (Linking)},
	author = {Ribeiro Ede, A., Jr. and Pinotsis, N. and Ghisleni, A. and Salmazo, A. and Konarev, P. V. and Kostan, J. and Sjoblom, B. and Schreiner, C. and Polyansky, A. A. and Gkougkoulia, E. A. and Holt, M. R. and Aachmann, F. L. and Zagrovic, B. and Bordignon, E. and Pirker, K. F. and Svergun, D. I. and Gautel, M. and Djinovic-Carugo, K.}
}
