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. 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.
journal_name
Celljournal_title
Cellauthors
Ribeiro Ede A Jr,Pinotsis N,Ghisleni A,Salmazo A,Konarev PV,Kostan J,Sjöblom B,Schreiner C,Polyansky AA,Gkougkoulia EA,Holt MR,Aachmann FL,Zagrović B,Bordignon E,Pirker KF,Svergun DI,Gautel M,Djinović-Carugo Kdoi
10.1016/j.cell.2014.10.056subject
Has Abstractpub_date
2014-12-04 00:00:00pages
1447-60issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(14)01428-7journal_volume
159pub_type
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