ArticleThe Journal of biological chemistry2010
Cystic fibrosis transmembrane conductance regulator interacts with multiple immunoglobulin domains of filamin A.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Could the Phenotypic Outcomes of Genetic Variability in Cells Operating in Mechanically Dynamic Environments be Influenced by a Disrupted "Cell-ECM" Relationship? Using Cystic Fibrosis and Marfan Syndrome as an Example.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- A Proteomic Survey of the Cystic Fibrosis Transmembrane Conductance Regulator Surfaceome.International journal of molecular sciences · 2023Review
- SARS-CoV-2 replication in airway epithelia requires motile cilia and microvillar reprogramming.Cell · 2023Article
- Congenital lung lesions: a radiographic pattern approach.Pediatric radiology · 2022Review
- Lipid-driven CFTR clustering is impaired in cystic fibrosis and restored by corrector drugs.Journal of cell science · 2022Article
- Blood co-expression modules identify potential modifier genes of diabetes and lung function in cystic fibrosis.PloS one · 2020Article
- Combining theoretical and experimental data to decipher CFTR 3D structures and functions.Cellular and molecular life sciences : CMLS · 2018Article
- An adventitious interaction of filamin A with RhoGDI2(Tyr153Glu).Biochemical and biophysical research communications · 2016Article
- Article
- Remodeling of the intestinal brush border underlies adhesion and virulence of an enteric pathogen.mBio · 2014Article
- A novel structural unit in the N-terminal region of filamins.The Journal of biological chemistry · 2014Article
- Article
- RACK1 interacts with filamin-A to regulate plasma membrane levels of the cystic fibrosis transmembrane conductance regulator.American journal of physiology. Cell physiology · 2013Article
- Filamin and phospholipase C-ε are required for calcium signaling in the Caenorhabditis elegans spermatheca.PLoS genetics · 2013Article
- Disruption of cytokeratin-8 interaction with F508del-CFTR corrects its functional defect.Human molecular genetics · 2012Article
- Filamins in mechanosensing and signaling.Annual review of biophysics · 2012Review
- Pro-prion binds filamin A, facilitating its interaction with integrin beta1, and contributes to melanomagenesis.The Journal of biological chemistry · 2010Article
- Biochemical basis of the interaction between cystic fibrosis transmembrane conductance regulator and immunoglobulin-like repeats of filamin.The Journal of biological chemistry · 2010Article
- The filamins: organizers of cell structure and function.Cell adhesion & migrationReview
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Authors and funding
7 authors.
Funding
Abstract
Mutations of the chloride channel cystic fibrosis transmembrane conductance regulator (CFTR) that impair its apical localization and function cause cystic fibrosis. A previous report has shown that filamin A (FLNa), an actin-cross-linking and -scaffolding protein, interacts directly with the cytoplasmic N terminus of CFTR and that this interaction is necessary for stability and confinement of the channel to apical membranes. Here, we report that the CFTR N terminus has sequence similarity to known FLNa-binding partner-binding sites. FLNa has 24 Ig (IgFLNa) repeats, and a CFTR peptide pulled down repeats 9, 12, 17, 19, 21, and 23, which share sequence similarity yet differ from the other FLNa Ig domains. Using known structures of IgFLNa.partner complexes as templates, we generated in silico models of IgFLNa.CFTR peptide complexes. Point and deletion mutants of IgFLNa and CFTR informed by the models, including disease-causing mutations L15P and W19C, disrupted the binding interaction. The model predicted that a P5L CFTR mutation should not affect binding, but a synthetic P5L mutant peptide had reduced solubility, suggesting a different disease-causing mechanism. Taken together with the fact that FLNa dimers are elongated ( approximately 160 nm) strands, whereas CFTR is compact (6 approximately 8 nm), we propose that a single FLNa molecule can scaffold multiple CFTR partners. Unlike previously defined dimeric FLNa.partner complexes, the FLNa-monomeric CFTR interaction is relatively weak, presumptively facilitating dynamic clustering of CFTR at cell membranes. Finally, we show that deletion of all CFTR interacting domains from FLNa suppresses the surface expression of CFTR on baby hamster kidney cells.
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