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Acute Perturbations in Golgi Organization Impact De Novo Sphingomyelin Synthesis
Author(s) -
Chandran Suchismita,
Machamer Carolyn E.
Publication year - 2008
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2008.00810.x
Subject(s) - golgi apparatus , endoplasmic reticulum , microbiology and biotechnology , ceramide , sphingomyelin , biology , golgi membrane , nocodazole , biochemistry , membrane , cell , cytoskeleton , apoptosis
The mammalian Golgi apparatus is composed of multiple stacks of cisternal membranes organized laterally into a ribbon‐like structure, with close apposition of trans Golgi regions with specialized endoplasmic reticulum (ER) membranes. These contacts may be the site of ceramide transfer from its site of synthesis (ER) to sphingomyelin (SM) synthase through ceramide transfer protein (CERT). CERT extracts ceramide from the ER and transfers it to Golgi membranes but the role of overall Golgi structure in this process is unknown. We show here that localization of CERT in puncta around the Golgi complex requires both ER‐ and Golgi‐binding domains of CERT. To examine how Golgi structure contributes to SM synthesis, we treated cells with Golgi‐perturbing drugs and measured newly synthesized SM. Interestingly, disruption of Golgi morphology with nocodazole, but not ilimaquinone inhibited SM synthesis. Decreased localization of CERT with a Golgi marker correlated with decreased SM synthesis. We propose that some Golgi structural perturbations interfere with efficient ceramide trafficking through CERT, and thus SM synthesis. The organization of the mammalian Golgi ribbon together with CERT may promote specific ER–Golgi interactions for efficient delivery of ceramide for SM synthesis.