ArticleCommunications biology2020
Phosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Genome-wide association study of mature cow size traits in American Angus cattle.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- AAV-Delivered RNAi Targeting Mutant LDB3 Prevents and Reverses Myofibrillar Myopathy through Mechanosignaling Restoration.bioRxiv : the preprint server for biology · 2026Article
- Haplotype GWAS in Swedish warmblood horses for conformation and jumping traits.Journal of animal science · 2026Article
- Aerobic and resistance exercise-regulated phosphoproteome and acetylproteome modifications in human skeletal muscle.Nature communications · 2025Article
- Filamin C dimerisation is regulated by HSPB7.Nature communications · 2025Article
- Article
- Identification of phosphatases that dephosphorylate the co-chaperone BAG3.Life science alliance · 2025Article
- Differential prolyl hydroxylation by six Physcomitrella prolyl-4 hydroxylases.Computational and structural biotechnology journal · 2024Article
- Protein phosphatase-1 regulates the binding of filamin C to FILIP1 in cultured skeletal muscle cells under mechanical stress.Scientific reports · 2024Article
- Identification of TFG- and Autophagy-Regulated Proteins and Glycerophospholipids in B Cells.Journal of proteome research · 2024Article
- Article
- Bi-allelic variants of FILIP1 cause congenital myopathy, dysmorphism and neurological defects.Brain : a journal of neurology · 2023Article
- GePI: large-scale text mining, customized retrieval and flexible filtering of gene/protein interactions.Nucleic acids research · 2023Article
- Filamin-A-interacting protein 1 (FILIP1) is a dual compartment protein linking myofibrils and microtubules during myogenic differentiation and upon mechanical stress.Cell and tissue research · 2023Article
- Homozygous loss-of-function variants in FILIP1 cause autosomal recessive arthrogryposis multiplex congenita with microcephaly.Human genetics · 2023Article
- Article
- Filamin C in cardiomyopathy: from physiological roles to DNA variants.Heart failure reviews · 2022Review
- Strain-induced mechanoresponse depends on cell contractility and BAG3-mediated autophagy.Molecular biology of the cell · 2021Article
- Maintaining proteostasis under mechanical stress.EMBO reports · 2021Review
- Evaluation of micropillar array columns for chromatographic separation of phosphorothioated oligonucleotides and their diastereomers.Analytical science advances · 2021Article
Corrections and comments
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Authors and funding
21 authors at 5 institutions in 2 countries.
Funding
Abstract
The PI3K/Akt pathway promotes skeletal muscle growth and myogenic differentiation. Although its importance in skeletal muscle biology is well documented, many of its substrates remain to be identified. We here studied PI3K/Akt signaling in contracting skeletal muscle cells by quantitative phosphoproteomics. We identified the extended basophilic phosphosite motif RxRxxp[S/T]xxp[S/T] in various proteins including filamin-C (FLNc). Importantly, this extended motif, located in a unique insert in Ig-like domain 20 of FLNc, is doubly phosphorylated. The protein kinases responsible for this dual-site phosphorylation are Akt and PKCα. Proximity proteomics and interaction analysis identified filamin A-interacting protein 1 (FILIP1) as direct FLNc binding partner. FILIP1 binding induces filamin degradation, thereby negatively regulating its function. Here, dual-site phosphorylation of FLNc not only reduces FILIP1 binding, providing a mechanism to shield FLNc from FILIP1-mediated degradation, but also enables fast dynamics of FLNc necessary for its function as signaling adaptor in cross-striated muscle cells.
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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.