ReviewThe Biochemical journal2024
Charting the importance of filamin A posttranslational modifications.
Review in The Biochemical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Development of a Nanoscale Protein-Protein Mapping of PDE4 Interface-Disrupting Peptides.Nano letters · 2026Article
- GutMGene-Guided Peripheral Blood Transcriptomics Identifies an FLNA-Associated Host-Gene Signal in Diabetic Retinopathy.International journal of molecular sciences · 2026Article
- Nuclear Proteome Map of Mouse Heart Chambers.Molecular & cellular proteomics : MCP · 2026Article
- Phosphorylated filamin-A at serine 1459 from plasma-derived small extracellular vesicles as a promising biomarker for high-risk adenoma and colorectal cancer.Scientific reports · 2026Article
- Defining the human lung pathodegradome of the V8 protease fromInfection and immunity · 2026Article
- ARHGAP21 enhances metastasis in hepatocellular carcinoma by inhibiting ubiquitination of filamin A.Cell death discovery · 2026Article
- Filamin A phosphorylation at S2152: a molecular switch fueling cancer and neurodegeneration.Cell communication and signaling : CCS · 2026Review
- Failed induction of human labour is associated with an altered myometrial phosphoproteome.Scientific reports · 2025Article
- Filamin A in focus: unravelling the multifaceted roles of filamin A in neurodevelopment and neurological disorders.Brain : a journal of neurology · 2025Review
- A Novel Subtype of Spondylocostal Dysplasia Associated With a Heterozygous Missense FLNA Variant.Orthopaedic surgery · 2025Article
- Endogenous SH2B1 protein localizes to lamellipodia and filopodia: platinum replica electron-microscopy study.microPublication biology · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Filamin A is an essential protein in the cell cytoskeleton because of its actin binding properties and unique homodimer rod-shaped structure, which organises actin into three-dimensional orthogonal networks imperative to cell motility, spreading and adhesion. Filamin A is subject to extensive posttranslational modification (PTM) which serves to co-ordinate cellular architecture and to modulate its large protein-protein interaction network which is key to the protein's role as a cellular signalling hub. Characterised PTMs include phosphorylation, irreversible cleavage, ubiquitin mediated degradation, hydroxylation and O-GlcNAcylation, with preliminary evidence of tyrosylation, carbonylation and acetylation. Each modification and its relation to filamin A function will be described here. These modifications are often aberrantly applied in a range of diseases including, but not limited to, cancer, cardiovascular disease and neurological disease and we discuss the concept of target specific PTMs with novel therapeutic modalities. In summary, our review represents a topical 'one-stop-shop' that enables understanding of filamin A function in cell homeostasis and provides insight into how a variety of modifications add an extra level of Filamin A control.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.