ArticleProceedings of the National Academy of Sciences of the United States of America2012
Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 29 citations in OpenAlex.
- Synaptic Vesicle Recycling and the Endolysosomal System: A Reappraisal of Form and Function.Frontiers in synaptic neuroscience · 2022Review
- Article
- Synaptic AP2 CCV life cycle regulation by the Eps15, ITSN1, Sgip1/AP2, synaptojanin1 interactome.Scientific reports · 2021Article
- Temporal Quantitative Proteomics of mGluR-induced Protein Translation and Phosphorylation in Neurons.Molecular & cellular proteomics : MCP · 2020Article
- Investigation of F-BAR domain PACSIN proteins uncovers membrane tubulation function in cilia assembly and transport.Nature communications · 2019Article
- ARHGAP42 is activated by Src-mediated tyrosine phosphorylation to promote cell motility.Journal of cell science · 2017Article
- Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017Review
- FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets.Blood · 2015Article
- Synaptic vesicle morphology: a case of protein sorting?Current opinion in cell biology · 2014Review
- PICK1 interacts with PACSIN to regulate AMPA receptor internalization and cerebellar long-term depression.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis.Open biology · 2013Article
- Phosphorylation of the Bin, Amphiphysin, and RSV161/167 (BAR) domain of ACAP4 regulates membrane tubulation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis.Molecular biology of the cell · 2013Article
- Membrane curvature and its generation by BAR proteins.Trends in biochemical sciences · 2012Review
- Article
- Defining the protein and lipid constituents of tubular recycling endosomes.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Syndapin I (PACSIN 1) is a synaptically enriched membrane tubulating protein that plays important roles in activity-dependent bulk endocytosis and neuronal morphogenesis. While syndapin I is an in vitro phosphoprotein, it is not known to be phosphorylated in neurons. Here, we report the identification of two phosphorylation sites, S76 and T181, of syndapin I from nerve terminals. Both residues are located at the N-terminal helix-capping motifs (N-Cap) of different α-helices in the F-BAR domain, important for F-BAR homodimer curvature and dimer-dimer filament assembly, respectively. Phospho-mimetic mutations of these residues regulate lipid-binding and tubulation both in vitro and in cells. Neither phosphosite regulated syndapin I function in activity-dependent bulk endocytosis. Rather, T181 phosphorylation was developmentally regulated and inhibited syndapin I function in neuronal morphogenesis. This suggests a novel mechanism for phosphorylation control of an F-BAR function through the regulation of α-helix interactions and stability within the folded F-BAR domain.
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