Ceramide chain length-dependent protein sorting into selective endoplasmic reticulum exit sites.

Ceramide chain length-dependent protein sorting into selective endoplasmic reticulum exit sites.
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DOI:
10.1126/sciadv.aba8237
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发表时间:
2020-12
期刊:
影响因子:
13.6
通讯作者:
Muñiz M
Muñiz M
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Rodriguez-Gallardo S;Kurokawa K;Sabido-Bozo S;Cortes-Gomez A;Ikeda A;Zoni V;Aguilera-Romero A;Perez-Linero AM;Lopez S;Waga M;Araki M;Nakano M;Riezman H;Funato K;Vanni S;Nakano A;Muñiz M

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3D high-resolution live imaging reveals the importance of ceramide chain length for protein sorting in selective export sites. Protein sorting in the secretory pathway is crucial to maintain cellular compartmentalization and homeostasis. In addition to coat-mediated sorting, the role of lipids in driving protein sorting during secretory transport is a longstanding fundamental question that still remains unanswered. Here, we conduct 3D simultaneous multicolor high-resolution live imaging to demonstrate in vivo that newly synthesized glycosylphosphatidylinositol-anchored proteins having a very long chain ceramide lipid moiety are clustered and sorted into specialized endoplasmic reticulum exit sites that are distinct from those used by transmembrane proteins. Furthermore, we show that the chain length of ceramide in the endoplasmic reticulum membrane is critical for this sorting selectivity. Our study provides the first direct in vivo evidence for lipid chain length–based protein cargo sorting into selective export sites of the secretory pathway.
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