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The Structure and Regulation of Human Muscle α-Actinin

Research output: Contribution to journalArticlepeer-review

Euripedes de Almeida Ribeiro, Nikos Pinotsis, Andrea Ghisleni, Anita Salmazo, Petr V Konarev, Julius Kostan, Björn Sjöblom, Claudia Schreiner, Anton A Polyansky, Eirini A Gkougkoulia, Mark R Holt, Finn L Aachmann, Bojan Zagrović, Enrica Bordignon, Katharina F Pirker, Dmitri I Svergun, Mathias Gautel, Kristina Djinović-Carugo

Original languageEnglish
Pages (from-to)1447-1460
Number of pages14
Issue number6
Early online date26 Nov 2014
Accepted/In press24 Oct 2014
E-pub ahead of print26 Nov 2014
Published4 Dec 2014


King's Authors


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. α-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 α-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.

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