ArticleThe Journal of biological chemistry2011
Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 80 citations in OpenAlex.
- Integrated molecular mechanisms of salinity response in Apostichopus japonicus: focus on miRNA-driven core pathways and target gene regulation.Marine biotechnology (New York, N.Y.) · 2026Review
- Phosphatidylinositol-4-phosphate signaling regulates dense granule biogenesis and maturation in Toxoplasma gondii.PLoS pathogens · 2026Article
- Article
- Discovery, Optimization, and Anticancer Activity of Lipid-Competitive Pleckstrin Homology Domain-Containing Family A Inhibitors.Journal of medicinal chemistry · 2025Article
- Assessing the Presence of Phosphoinositides on Autophagosomal Membrane in Yeast by Live Cell Imaging.Microorganisms · 2024Article
- The C10orf76-PI4KB axis orchestrates CERT-mediated ceramide trafficking to the distal Golgi.The Journal of cell biology · 2023Article
- Sphingolipids mediate polar sorting of PIN2 through phosphoinositide consumption at the trans-Golgi network.Nature communications · 2021Article
- Interaction of the N terminus of ADP-ribosylation factor with the PH domain of the GTPase-activating protein ASAP1 requires phosphatidylinositol 4,5-bisphosphate.The Journal of biological chemistry · 2019Article
- Lipid-dependent coupling of secretory cargo sorting and trafficking at the trans-Golgi network.FEBS letters · 2019Review
- A dual role for cell plate-associated PI4Kβ in endocytosis and phragmoplast dynamics during plant somatic cytokinesis.The EMBO journal · 2019Article
- Tethering of Multi-Vesicular Bodies and the Tonoplast to the Plasma Membrane in Plants.Frontiers in plant science · 2019Article
- Manipulating Endoplasmic Reticulum-Plasma Membrane Tethering in Plants Through Fluorescent Protein Complementation.Frontiers in plant science · 2019Article
- Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites.Journal of lipid research · 2018Review
- The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis.Molecular biology of the cell · 2018Article
- A Golgi Lipid Signaling Pathway Controls Apical Golgi Distribution and Cell Polarity during Neurogenesis.Developmental cell · 2018Article
- Article
- PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions.Journal of visualized experiments : JoVE · 2017Article
- Sphingolipid metabolic flow controls phosphoinositide turnover at theThe EMBO journal · 2017Article
- Interactions of Pleckstrin Homology Domains with Membranes: Adding Back the Bilayer via High-Throughput Molecular Dynamics.Structure (London, England : 1993) · 2016Article
- A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants.Nature plants · 2016Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
Four-phosphate-adaptor protein 1 (FAPP1) regulates secretory transport from the trans-Golgi network (TGN) to the plasma membrane. FAPP1 is recruited to the Golgi through binding of its pleckstrin homology (PH) domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). Despite the critical role of FAPP1 in membrane trafficking, the molecular basis of its dual function remains unclear. Here, we report a 1.9 Å resolution crystal structure of the FAPP1 PH domain and detail the molecular mechanisms of the PtdIns(4)P and ARF1 recognition. The FAPP1 PH domain folds into a seven-stranded β-barrel capped by an α-helix at one edge, whereas the opposite edge is flanked by three loops and the β4 and β7 strands that form a lipid-binding pocket within the β-barrel. The ARF1-binding site is located on the outer side of the β-barrel as determined by NMR resonance perturbation analysis, mutagenesis, and measurements of binding affinities. The two binding sites have little overlap, allowing FAPP1 PH to associate with both ligands simultaneously and independently. Binding to PtdIns(4)P is enhanced in an acidic environment and is required for membrane penetration and tubulation activity of FAPP1, whereas the GTP-bound conformation of the GTPase is necessary for the interaction with ARF1. Together, these findings provide structural and biochemical insight into the multivalent membrane anchoring by the PH domain that may augment affinity and selectivity of FAPP1 toward the TGN membranes enriched in both PtdIns(4)P and GTP-bound ARF1.
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