Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20–21
Seppälä, J., Tossavainen, H., Rodic, N., Permi, P., Pentikäinen, U., & Ylänne, J. (2015). Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20–21. PLoS ONE, 10(8), Article e0136969. https://doi.org/10.1371/journal.pone.0136969
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2015Copyright
© 2015 Seppälä et al. This is an open
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credited.
Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions.
Besides regulating the actin cytoskeleton, they serve as important links between the extracellular
matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds
for signaling proteins, and binding several other cytoskeletal proteins that regulate cell
adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding
domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated
that myosin-mediated contractile forces can reveal hidden protein binding sites in
the domain pairs IgFLNa18–19 and 20–21, enabling FLNs to transduce mechanical signals
in cells. The atomic structures of these mechanosensor domain pairs in the resting state are
known, as well as the structures of individual IgFLN21 with ligand peptides. However, little
experimental data is available on how interacting protein binding deforms the domain pair
structures. Here, using small-angle x-ray scattering-based modelling, x-ray crystallography,
and NMR, we show that the adaptor protein migfilin-derived peptide-bound structure of
IgFLNa20–21 is flexible and adopts distinctive conformations depending on the presence or
absence of the interacting peptide. The conformational changes reported here may be common
for all peptides and may play a role in the mechanosensor function of the site.
...
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Except where otherwise noted, this item's license is described as © 2015 Seppälä et al. This is an open
access article distributed under the terms of the
Creative Commons Attribution License, which permits
unrestricted use, distribution, and reproduction in any
medium, provided the original author and source are
credited.
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