title: Small-angle X-ray scattering reveals compact domain-domain interactions in the N-terminal region of filamin C.
abstract: Filamins are multi-domain, actin cross-linking, and scaffolding proteins. In addition to the actin cross-linking function, filamins have a role in mechanosensor signaling. The mechanosensor function is mediated by domain-domain interaction in the C-terminal region of filamins. Recently, we have shown that there is a three-domain interaction module in the N-terminal region of filamins, where the neighboring domains stabilize the structure of the middle domain and thereby regulate its interaction with ligands. In this study, we have used small-angle X-ray scattering as a tool to screen for potential domain-domain interactions in the N-terminal region. We found evidence of four domain-domain interactions with varying flexibility. These results confirm our previous study showing that domains 3, 4, and 5 exist as a compact three domain module. In addition, we report interactions between domains 11-12 and 14-15, which are thus new candidate sites for mechanical regulation.
authors.affiliation: Department of Biological and Environmental Science and Nanoscience Center, University of Jyväskylä, Jyväskylä, Finland.
authors.forename: Ritika
authors.initials: R
authors.lastname: Sethi
authors.affiliation: Department of Biological and Environmental Science and Nanoscience Center, University of Jyväskylä, Jyväskylä, Finland.
authors.forename: Jari
authors.initials: J
authors.lastname: Ylänne
mesh_terms: D064448:Filamins / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction
chemical_list: D064448:Filamins