ArticleNature communications2019
Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed, 144 citations in OpenAlex.
- Spatial organization of phosphoinositide signaling.FEBS letters · 2026Review
- The lipid-binding PX domain of RRC-1 (ARHGAP32/33) is required for optimal assembly and function of integrin adhesion complexes at the muscle cell boundary in C. elegans.G3 (Bethesda, Md.) · 2026Article
- Structural Organization of the Nvj3-Mdm1 Complex Reveals a Conserved Lipid-Compatible Contact Site Module.bioRxiv : the preprint server for biology · 2026Article
- Cell surface liposome binding (CLiB) allows lipid-binding probe engineering via high-throughput screening.Nature cell biology · 2026Article
- The Lipid-binding PX Domain of RRC-1 (ARHGAP32/33) is Required for Optimal Assembly and Function of Integrin Adhesion Complexes at the Muscle Cell Boundary in C. elegans.bioRxiv : the preprint server for biology · 2025Article
- Bi-allelic variants in the ribosomal protein RPS6KC1 cause a complex neurodevelopmental disorder.American journal of human genetics · 2025Article
- PI(3)P coordinates SNX17- and SNX27-dependent protein recycling for long-term synaptic plasticity.The Journal of cell biology · 2025Article
- Characterization of a phosphoinositide-binding protein containing a PHOX homology domain in the malaria parasite Plasmodium falciparum.Scientific reports · 2025Article
- Dual SLIPT-A Lipid Mimic to Enable Spatiotemporally Defined, Sequential Protein Dimerization.ACS chemical biology · 2025Article
- SNX10 functions as a modulator of piecemeal mitophagy and mitochondrial bioenergetics.The Journal of cell biology · 2025Article
- Membrane composition and curvature in SNX9-mediated actin polymerization.Molecular biology of the cell · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- SNX19 Interacts with Caveolin-1 and Flotillin-1 to Regulate DBiomedicines · 2025Article
- VARP binds SNX27 to promote endosomal supercomplex formation on membranes.Science advances · 2025Article
- A Complex Interplay Between Melatonin and RORβ: RORβ is Unlikely a Putative Receptor for Melatonin as Revealed by Biophysical Assays.Molecular neurobiology · 2025Article
- Phosphoinositide signaling in the nucleus: Impacts on chromatin and transcription regulation.Biology of the cell · 2025Review
- Use of Bio-Layer Interferometry (BLI) to Measure Binding Affinities of SNAREs and Phosphoinositides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Exploring potential causal genetic variants and genes for endometrial cancer: Open Targets Genetics, Mendelian randomization, and multi-tissue transcriptome-wide association analysis.Translational cancer research · 2024Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- VARP binds SNX27 to promote endosomal supercomplex formation on membranes.bioRxiv : the preprint server for biology · 2024Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
16 authors at 3 institutions in 3 countries.
Funding
Abstract
Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family.
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