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- W2978904081 abstract "Protein trafficking requires coat complexes that couple recognition of sorting motifs in transmembrane cargoes with biogenesis of transport carriers. The mechanisms of cargo transport through the endosomal network are poorly understood. Here, we identify a sorting motif for endosomal recycling of cargoes, including the cation-independent mannose-6-phosphate receptor and semaphorin 4C, by the membrane tubulating BAR domain-containing sorting nexins SNX5 and SNX6. Crystal structures establish that this motif folds into a β-hairpin, which binds a site in the SNX5/SNX6 phox homology domains. Over sixty cargoes share this motif and require SNX5/SNX6 for their recycling. These include cargoes involved in neuronal migration and a Drosophila snx6 mutant displays defects in axonal guidance. These studies identify a sorting motif and provide molecular insight into an evolutionary conserved coat complex, the 'Endosomal SNX-BAR sorting complex for promoting exit 1' (ESCPE-1), which couples sorting motif recognition to the BAR-domain-mediated biogenesis of cargo-enriched tubulo-vesicular transport carriers." @default.
- W2978904081 created "2019-10-10" @default.
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- W2978904081 date "2019-10-01" @default.
- W2978904081 modified "2023-10-08" @default.
- W2978904081 title "Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins" @default.
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- W2978904081 doi "https://doi.org/10.1038/s41556-019-0393-3" @default.
- W2978904081 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6778059" @default.
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- W2978904081 hasPublicationYear "2019" @default.
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