高尔基体
神经酰胺
鞘脂
内质网
生物
细胞生物学
生物化学
细胞凋亡
作者
Sergej Limar,Carolin Körner,Fernando Martínez-Montañés,Viktoriya Stancheva,Verena N. Wolf,Stefan Walter,Elizabeth A. Miller,Christer S. Ejsing,Vanesa V. Galassi,Florian Fröhlich
出处
期刊:PubMed
日期:2023-05-01
卷期号:222 (5)
被引量:11
标识
DOI:10.1083/jcb.202109162
摘要
Ceramides are essential precursors of complex sphingolipids and act as potent signaling molecules. Ceramides are synthesized in the endoplasmic reticulum (ER) and receive their head-groups in the Golgi apparatus, yielding complex sphingolipids (SPs). Transport of ceramides between the ER and the Golgi is executed by the essential ceramide transport protein (CERT) in mammalian cells. However, yeast cells lack a CERT homolog, and the mechanism of ER to Golgi ceramide transport remains largely elusive. Here, we identified a role for yeast Svf1 in ceramide transport between the ER and the Golgi. Svf1 is dynamically targeted to membranes via an N-terminal amphipathic helix (AH). Svf1 binds ceramide via a hydrophobic binding pocket that is located in between two lipocalin domains. We showed that Svf1 membrane-targeting is important to maintain flux of ceramides into complex SPs. Together, our results show that Svf1 is a ceramide binding protein that contributes to sphingolipid metabolism at Golgi compartments.
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