Proteomics

Dataset Information

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


ABSTRACT: Protein trafficking requires coat complexes that couple recognition of sorting motifs in transmembrane cargos 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 cargos 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 that binds a site in the SNX5/SNX6 phox homology domains. Over sixty cargos share this motif and require SNX5/SNX6 for their recycling. These include cargos 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 BAR domain-mediated biogenesis of cargo-enriched tubulo-vesicular transport carriers.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Hela Cell

SUBMITTER: Boris Simonetti  

LAB HEAD: Pete Cullen

PROVIDER: PXD014927 | Pride | 2021-05-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Interactome9PlexTMT_Grouped_PS.msf Msf
Interactome9PlexTMT_IndividualSamples_PS.msf Msf
InteractomeBlankPreRpt.raw Raw
InteractomeBlankPreRun.msf Msf
InteractomeBlankPreRun.raw Raw
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Publications

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

Simonetti Boris B   Paul Blessy B   Chaudhari Karina K   Weeratunga Saroja S   Weeratunga Saroja S   Steinberg Florian F   Gorla Madhavi M   Heesom Kate J KJ   Bashaw Greg J GJ   Collins Brett M BM   Cullen Peter J PJ  

Nature cell biology 20191001 10


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  ...[more]

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