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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.

SUBMITTER: Sethi R

PROVIDER: S-EPMC4170960 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Small-angle X-ray scattering reveals compact domain-domain interactions in the N-terminal region of filamin C.

Sethi Ritika R Ylänne Jari J

PloS one 20140922 9

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 ...[more]

PMID: 25243668

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