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Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)1219-1233
Number of pages15
JournalNature Cell Biology
Volume21
DOIs
DateAccepted/In press - 19 Aug 2019
DatePublished (current) - 1 Oct 2019

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.

    Research areas

  • endosomes, membrane trafficking, structural biology

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Documents

  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Nature Research at https://www.nature.com/articles/s41556-019-0393-3. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 165 MB, PDF document

DOI

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