ArticlePloS one2014
Small-angle X-ray scattering reveals compact domain-domain interactions in the N-terminal region of filamin C.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- TheBiomedicines · 2024Article
- Pathogen-specific structural features ofmBio · 2023Article
- Structure and Function of Filamin C in the Muscle Z-Disc.International journal of molecular sciences · 2020Review
- Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.Biophysical journal · 2019Article
- Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.Structure (London, England : 1993) · 2019Article
- CDC42 binds PAK4 via an extended GTPase-effector interface.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains.Scientific reports · 2017Article
- Evidence for the mechanosensor function of filamin in tissue development.Scientific reports · 2016Article
- MVP-Associated Filamin A Mutations Affect FlnA-PTPN12 (PTP-PEST) Interactions.Journal of cardiovascular development and disease · 2015Article
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Authors and funding
2 authors.
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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.
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