ArticlePloS one2009
Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 76 citations in OpenAlex.
- Uncovering minimal pathways in melanoma initiation.Nature communications · 2025Article
- The Role of Mechanotransduction in Contact Inhibition of Locomotion and Proliferation.International journal of molecular sciences · 2024Review
- Article
- FilGAP regulates tumor growth in Glioma through the regulation of mTORC1 and mTORC2.Scientific reports · 2023Article
- Isoform-specific roles of the Drosophila filamin-type protein Jitterbug (Jbug) during development.Genetics · 2021Article
- Structure and Function of Filamin C in the Muscle Z-Disc.International journal of molecular sciences · 2020Review
- Molecular Tuning of Filamin A Activities in the Context of Adhesion and Migration.Frontiers in cell and developmental biology · 2020Review
- Identification of the Six-RNA-Binding Protein Signature for Prognosis Prediction in Bladder Cancer.Frontiers in genetics · 2020Article
- Filamin A regulates EGFR/ERK/Akt signaling and affects colorectal cancer cell growth and migration.Molecular medicine reports · 2019Article
- DYT1 Dystonia Patient-Derived Fibroblasts Have Increased Deformability and Susceptibility to Damage by Mechanical Forces.Frontiers in cell and developmental biology · 2019Article
- Comparative analysis of the two extremes ofAmerican journal of translational research · 2018Article
- Skeletal Dysplasia Mutations Effect on Human Filamins' Structure and Mechanosensing.Scientific reports · 2017Article
- Structural and thermodynamic basis of a frontometaphyseal dysplasia mutation in filamin A.The Journal of biological chemistry · 2017Article
- Mechanotransduction Mechanisms in Mitral Valve Physiology and Disease Pathogenesis.Frontiers in cardiovascular medicine · 2017Review
- An adventitious interaction of filamin A with RhoGDI2(Tyr153Glu).Biochemical and biophysical research communications · 2016Article
- Cyclic Mechanical Loading Is Essential for Rac1-Mediated Elongation and Remodeling of the Embryonic Mitral Valve.Current biology : CB · 2016Article
- Src Family Tyrosine Kinase Signaling Regulates FilGAP through Association with RBM10.PloS one · 2016Article
- Phosphorylation of Serine 402 Regulates RacGAP Protein Activity of FilGAP Protein.The Journal of biological chemistry · 2015Article
- MVP-Associated Filamin A Mutations Affect FlnA-PTPN12 (PTP-PEST) Interactions.Journal of cardiovascular development and disease · 2015Article
- Diverse phenotypic consequences of mutations affecting the C-terminus of FLNA.Journal of molecular medicine (Berlin, Germany) · 2015Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundMutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans. METHODOLOGY/PRINCIPAL
findingsWe determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell polarity and movement, and the effect of the three disease-related mutations on this interaction. A combination of NMR structural analysis and in silico modeling revealed the structural interface details between the C and D beta-strands of the IgFLNa23 and the C-terminal 32 residues of FilGAP. Mutagenesis of the predicted key interface residues confirmed the binding constraints between the two proteins. Specific loss-of-function FLNa constructs were generated and used to analyze the importance of the FLNa-FilGAP interaction in vivo. Point mutagenesis revealed that disruption of the FLNa-FilGAP interface perturbs cell spreading. FilGAP does not bind FLNa homologs FLNb or FLNc establishing the importance of this interaction to the human FLNa mutations. Tight complex formation requires dimerization of both partners and the correct alignment of the binding surfaces, which is promoted by a flexible hinge domain between repeats 23 and 24 of FLNa. FLNa mutations associated with human developmental anomalies disrupt the binding interaction and weaken the elasticity of FLNa/F-actin network under high mechanical stress. CONCLUSIONS/SIGNIFICANCE: Mutational analysis informed by structure can generate reagents for probing specific cellular interactions of FLNa. Disease-related FLNa mutations have demonstrable effects on FLNa function.
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Registered trials
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