ArticleAdvances in biological regulation2022
Biochemical basis for an interaction between SNX27 and the flexible SNX1 N-terminus.
Article in Advances in biological regulation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Structural mechanisms of cargo adaptors in membrane trafficking.Current opinion in cell biology · 2026Review
- Hybrid endosomal coats contain different classes of sorting nexins.The EMBO journal · 2026Article
- Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation.Nature communications · 2025Article
- Separation of powers: A key feature underlying the neuroprotective role of Retromer in age-related neurodegenerative disease?Current opinion in cell biology · 2025Review
- 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
- VARP binds SNX27 to promote endosomal supercomplex formation on membranes.bioRxiv : the preprint server for biology · 2024Article
- N-terminal signals in the SNX-BAR paralogs Vps5 and Vin1 guide endosomal coat complex formation.Molecular biology of the cell · 2024Article
- Architecture of the ESCPE-1 membrane coat.Nature structural & molecular biology · 2023Article
- Out of the ESCPE room: Emerging roles of endosomal SNX-BARs in receptor transport and host-pathogen interaction.Traffic (Copenhagen, Denmark) · 2023Review
- An interaction between β'-COP and the ArfGAP, Glo3, maintains post-Golgi cargo recycling.The Journal of cell biology · 2023Article
- Review
- SNX27-Retromer directly binds ESCPE-1 to transfer cargo proteins during endosomal recycling.PLoS biology · 2022Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Metazoans require the sorting nexin (SNX) protein, SNX27, to recycle hundreds of important transmembrane protein receptors from endosomes to the plasma membrane. Cargo recycling by SNX27 requires its interaction with retromer, a heterotrimer known to assemble on membranes with multiple sorting nexins, including SNX-BAR proteins and SNX3. SNX27 has also been functionally linked to SNX-BARs, but the molecular basis of this interaction has been unknown. We identify a direct biochemical interaction between the conserved and flexible SNX1/SNX2 N-terminus and full-length SNX27 using purified proteins in pulldown experiments. Sequence alignments indicate both SNX1 and SNX2 contain two short and conserved stretches of acidic residues bearing a DxF motif in their flexible N-terminal regions. Biochemical pulldown and mapping experiments reveal forty residues in the N-terminus of either SNX1 or SNX2 can mediate binding to SNX27. SNX27 truncation analysis demonstrates the SNX27 FERM domain binds the SNX1 N-terminus. Calorimetry experiments quantified binding between the SNX1 N-terminus and SNX27 in the low micromolar affinity range (K
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.