ArticleJournal of cell science2015
Phosphoinositide binding by the SNX27 FERM domain regulates its localization at the immune synapse of activated T-cells.
Article in Journal of cell science, 2015. 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.
- Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- OCRL1 Deficiency Affects the Intracellular Traffic of ApoER2 and Impairs Reelin-Induced Responses.Biomolecules · 2024Article
- Review
- Receptor Recycling by Retromer.Molecular and cellular biology · 2023Review
- Review
- SNX27-Retromer directly binds ESCPE-1 to transfer cargo proteins during endosomal recycling.PLoS biology · 2022Article
- SNX27 suppresses SARS-CoV-2 infection by inhibiting viral lysosome/late endosome entry.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Identification of a lncRNA AC011511.5- Mediated Competitive Endogenous RNA Network Involved in the Pathogenesis of Allergic Rhinitis.Frontiers in genetics · 2022Article
- Retromer dependent changes in cellular homeostasis and Parkinson's disease.Essays in biochemistry · 2021Review
- De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex.Science advances · 2021Article
- SNX27-FERM-SNX1 complex structure rationalizes divergent trafficking pathways by SNX17 and SNX27.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- F-Actin Dynamics in the Regulation of Endosomal Recycling and Immune Synapse Assembly.Frontiers in cell and developmental biology · 2021Review
- Toward Understanding the Molecular Role of SNX27/Retromer in Human Health and Disease.Frontiers in cell and developmental biology · 2021Review
- Interplay Between SNX27 and DAG Metabolism in the Control of Trafficking and Signaling at the IS.International journal of molecular sciences · 2020Review
- Sorting nexin 27 (SNX27) regulates the trafficking and activity of the glutamine transporter ASCT2.The Journal of biological chemistry · 2018Article
- GPCR Signaling and Trafficking: The Long and Short of It.Trends in endocrinology and metabolism: TEM · 2017Review
- Article
- A molecular code for endosomal recycling of phosphorylated cargos by the SNX27-retromer complex.Nature structural & molecular biology · 2016Article
- Role of the Retromer Complex in Neurodegenerative Diseases.Frontiers in aging neuroscience · 2016Review
- Structure and Membrane Binding Properties of the Endosomal Tetratricopeptide Repeat (TPR) Domain-containing Sorting Nexins SNX20 and SNX21.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sorting nexin 27 (SNX27) controls the endosomal-to-cell-surface recycling of diverse transmembrane protein cargos. Crucial to this function is the recruitment of SNX27 to endosomes which is mediated by the binding of phosphatidylinositol-3-phosphate (PtdIns3P) by its phox homology (PX) domain. In T-cells, SNX27 localizes to the immunological synapse in an activation-dependent manner, but the molecular mechanisms underlying SNX27 translocation remain to be clarified. Here, we examined the phosphoinositide-lipid-binding capabilities of full-length SNX27, and discovered a new PtdInsP-binding site within the C-terminal 4.1, ezrin, radixin, moesin (FERM) domain. This binding site showed a clear preference for bi- and tri-phosphorylated phophoinositides, and the interaction was confirmed through biophysical, mutagenesis and modeling approaches. At the immunological synapse of activated T-cells, cell signaling regulates phosphoinositide dynamics, and we find that perturbing phosphoinositide binding by the SNX27 FERM domain alters the SNX27 distribution in both endosomal recycling compartments and PtdIns(3,4,5)P3-enriched domains of the plasma membrane during synapse formation. Our results suggest that SNX27 undergoes dynamic partitioning between different membrane domains during immunological synapse assembly, and underscore the contribution of unique lipid interactions for SNX27 orchestration of cargo trafficking.
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