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

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Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins. / Simonetti, Boris; Paul, Blessy; Chaudhari, Katrina; Weeratunga, Soroja; Steinberg, Florian; Gorla, Madhavi; Heesom, Kate J; Bashaw, Greg; Collins, Brett; Cullen, Peter J.

In: Nature Cell Biology, Vol. 21, 01.10.2019, p. 1219–1233.

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Simonetti, B, Paul, B, Chaudhari, K, Weeratunga, S, Steinberg, F, Gorla, M, Heesom, KJ, Bashaw, G, Collins, B & Cullen, PJ 2019, 'Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins', Nature Cell Biology, vol. 21, pp. 1219–1233. https://doi.org/10.1038/s41556-019-0393-3

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Vancouver

Simonetti B, Paul B, Chaudhari K, Weeratunga S, Steinberg F, Gorla M et al. Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins. Nature Cell Biology. 2019 Oct 1;21:1219–1233. https://doi.org/10.1038/s41556-019-0393-3

Author

Simonetti, Boris ; Paul, Blessy ; Chaudhari, Katrina ; Weeratunga, Soroja ; Steinberg, Florian ; Gorla, Madhavi ; Heesom, Kate J ; Bashaw, Greg ; Collins, Brett ; Cullen, Peter J. / Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins. In: Nature Cell Biology. 2019 ; Vol. 21. pp. 1219–1233.

Bibtex

@article{3c49191b131d4d409e7dfb327b4a8d98,
title = "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 intoan 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",
author = "Boris Simonetti and Blessy Paul and Katrina Chaudhari and Soroja Weeratunga and Florian Steinberg and Madhavi Gorla and Heesom, {Kate J} and Greg Bashaw and Brett Collins and Cullen, {Peter J}",
year = "2019",
month = "10",
day = "1",
doi = "10.1038/s41556-019-0393-3",
language = "English",
volume = "21",
pages = "1219–1233",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Springer Nature",

}

RIS - suitable for import to EndNote

TY - JOUR

T1 - Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins

AU - Simonetti, Boris

AU - Paul, Blessy

AU - Chaudhari, Katrina

AU - Weeratunga, Soroja

AU - Steinberg, Florian

AU - Gorla, Madhavi

AU - Heesom, Kate J

AU - Bashaw, Greg

AU - Collins, Brett

AU - Cullen, Peter J

PY - 2019/10/1

Y1 - 2019/10/1

N2 - 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 intoan 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

AB - 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 intoan 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

U2 - 10.1038/s41556-019-0393-3

DO - 10.1038/s41556-019-0393-3

M3 - Article

VL - 21

SP - 1219

EP - 1233

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

ER -