ArticleProceedings of the National Academy of Sciences of the United States of America2021
SNX27-FERM-SNX1 complex structure rationalizes divergent trafficking pathways by SNX17 and SNX27.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
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47 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.
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- Structural mechanisms of cargo adaptors in membrane trafficking.Current opinion in cell biology · 2026Review
- SNX-mediated biogenesis of a plant-unique vesicle derived from the multivesicular body.Nature communications · 2026Article
- Sorting nexin 5 mediates antigen presentation and immunity againstbioRxiv : the preprint server for biology · 2026Article
- PI(3)P coordinates SNX17- and SNX27-dependent protein recycling for long-term synaptic plasticity.The Journal of cell biology · 2025Article
- Genetic Adaptation to Brackish Water and Spawning Season in European Cisco.Molecular ecology · 2025Article
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- Identification of a VPS29 isoform with restricted association to Retriever and Retromer accessory proteins through autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Separation of powers: A key feature underlying the neuroprotective role of Retromer in age-related neurodegenerative disease?Current opinion in cell biology · 2025Review
- Molecular basis for the assembly of the Vps5-Vps17 SNX-BAR proteins with Retromer.Nature communications · 2025Article
- VARP binds SNX27 to promote endosomal supercomplex formation on membranes.Science advances · 2025Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Contrasting Retromer with a Newly Described Retriever inPlants (Basel, Switzerland) · 2024Review
- 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
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- VARP binds SNX27 to promote endosomal supercomplex formation on membranes.bioRxiv : the preprint server for biology · 2024Article
- Metabolic reprogramming in astrocytes results in neuronal dysfunction in intellectual disability.Molecular psychiatry · 2024Article
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
The molecular events that determine the recycling versus degradation fates of internalized membrane proteins remain poorly understood. Two of the three members of the SNX-FERM family, SNX17 and SNX31, utilize their FERM domain to mediate endocytic trafficking of cargo proteins harboring the NPxY/NxxY motif. In contrast, SNX27 does not recycle NPxY/NxxY-containing cargo but instead recycles cargo containing PDZ-binding motifs via its PDZ domain. The underlying mechanism governing this divergence in FERM domain binding is poorly understood. Here, we report that the FERM domain of SNX27 is functionally distinct from SNX17 and interacts with a novel DLF motif localized within the N terminus of SNX1/2 instead of the NPxY/NxxY motif in cargo proteins. The SNX27-FERM-SNX1 complex structure reveals that the DLF motif of SNX1 binds to a hydrophobic cave surrounded by positively charged residues on the surface of SNX27. The interaction between SNX27 and SNX1/2 is critical for efficient SNX27 recruitment to endosomes and endocytic recycling of multiple cargoes. Finally, we show that the interaction between SNX27 and SNX1/2 is critical for brain development in zebrafish. Altogether, our study solves a long-standing puzzle in the field and suggests that SNX27 and SNX17 mediate endocytic recycling through fundamentally distinct mechanisms.
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