期刊
NATURE
卷 501, 期 7465, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature12423
关键词
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资金
- Telethon [GSP08002, GGP06166]
- Associazione Italiana per la Ricerca sul Cancro (AIRC) [IG 8623]
- EU (FP7 Lipidomicnet)
- AIRC [MFAG 10585]
- Academy of Finland
- Sigrid Juselius Foundation
- Study Abroad Scholarship from the Taiwan Ministry of Education
- Grants-in-Aid for Scientific Research [25113517, 23591347, 24659084, 24390046] Funding Source: KAKEN
- British Heart Foundation [PG/11/109/29247] Funding Source: researchfish
- Medical Research Council [MC_U105184308] Funding Source: researchfish
- MRC [MC_U105184308] Funding Source: UKRI
Newly synthesized proteins and lipids are transported across the Golgi complex via different mechanisms whose respective roles are not completely clear. We previously identified a non-vesicular intra-Golgi transport pathway for glucosylceramide (GlcCer)-the common precursor of the different series of glycosphingolipids-that is operated by the cytosolic GlcCer-transfer protein FAPP2 (also known as PLEKHA8) (ref. 1). However, the molecular determinants of the FAPP2-mediated transfer of GlcCer from the cis-Golgi to the trans-Golgi network, as well as the physiological relevance of maintaining two parallel transport pathways of GlcCer-vesicular and non-vesicular-through the Golgi, remain poorly defined. Here, using mouse and cell models, we clarify the molecular mechanisms underlying the intra-Golgi vectorial transfer of GlcCer by FAPP2 and show that GlcCer is channelled by vesicular and non-vesicular transport to two topologically distinct glycosylation tracks in the Golgi cisternae and the trans-Golgi network, respectively. Our results indicate that the transport modality across the Golgi complex is a key determinant for the glycosylation pattern of a cargo and establish a new paradigm for the branching of the glycosphingolipid synthetic pathway.
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