ArticleThe Journal of biological chemistry2014
A novel structural unit in the N-terminal region of filamins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- The Role of Mechanotransduction in Contact Inhibition of Locomotion and Proliferation.International journal of molecular sciences · 2024Review
- TheBiomedicines · 2024Article
- Rare clinical phenotype of filaminopathy presenting as restrictive cardiomyopathy and myopathy in childhood.Orphanet journal of rare diseases · 2022Article
- Article
- Structure and Function of Filamin C in the Muscle Z-Disc.International journal of molecular sciences · 2020Review
- Clinical exome sequencing revealed that FLNC variants contribute to the early diagnosis of cardiomyopathies in infant patients.Translational pediatrics · 2020Article
- 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
- Combining theoretical and experimental data to decipher CFTR 3D structures and functions.Cellular and molecular life sciences : CMLS · 2018Article
- Skeletal Dysplasia Mutations Effect on Human Filamins' Structure and Mechanosensing.Scientific reports · 2017Article
- Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains.Scientific reports · 2017Article
- MVP-Associated Filamin A Mutations Affect FlnA-PTPN12 (PTP-PEST) Interactions.Journal of cardiovascular development and disease · 2015Article
- Article
- Small-angle X-ray scattering reveals compact domain-domain interactions in the N-terminal region of filamin C.PloS one · 2014Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin-like (Ig) domains are a widely expanded superfamily that act as interaction motifs or as structural spacers in multidomain proteins. Vertebrate filamins (FLNs), which are multifunctional actin-binding proteins, consist of 24 Ig domains. We have recently discovered that in the C-terminal rod 2 region of FLN, Ig domains interact with each other forming functional domain pairs, where the interaction with signaling and transmembrane proteins is mechanically regulated by weak actomyosin contraction forces. Here, we investigated if there are similar inter-domain interactions around domain 4 in the N-terminal rod 1 region of FLN. Protein crystal structures revealed a new type of domain organization between domains 3, 4, and 5. In this module, domains 4 and 5 interact rather tightly, whereas domain 3 has a partially flexible interface with domain 4. NMR peptide titration experiments showed that within the three-domain module, domain 4 is capable for interaction with a peptide derived from platelet glycoprotein Ib. Crystal structures of FLN domains 4 and 5 in complex with the peptide revealed a typical β sheet augmentation interaction observed for many FLN ligands. Domain 5 was found to stabilize domain 4, and this could provide a mechanism for the regulation of domain 4 interactions.
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