TY  - JOUR
AU  - Ribeiro, Euripedes de Almeida
AU  - Pinotsis, Nikos
AU  - Ghisleni, Andrea
AU  - Salmazo, Anita
AU  - Konarev, Petr
AU  - Kostan, Julius
AU  - Sjöblom, Björn
AU  - Schreiner, Claudia
AU  - Polyansky, Anton A.
AU  - Gkougkoulia, Eirini A.
AU  - Holt, Mark R.
AU  - Aachmann, Finn L.
AU  - Žagrović, Bojan
AU  - Bordignon, Enrica
AU  - Pirker, Katharina F.
AU  - Svergun, Dmitri
AU  - Gautel, Mathias
AU  - Djinović-Carugo, Kristina
TI  - The Structure and Regulation of Human Muscle α-Actinin
JO  - Cell
VL  - 159
IS  - 6
SN  - 0092-8674
CY  - [Cambridge, Mass.]
PB  - Cell Press
M1  - PUBDB-2015-01323
SP  - 1447 - 1460
PY  - 2014
N1  - OA
AB  - 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
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000346652900021
C6  - pmid:25433700
DO  - DOI:10.1016/j.cell.2014.10.056
UR  - https://bib-pubdb1.desy.de/record/207413
ER  -