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Targeted Sphingolipid analysis of HeLa knockout for expression of GRASP55

ABSTRACT: Golgi apparatus, the main glycosylation station of the cell, consists of a stack of discontinuous cisternae. Glycosylation enzymes are usually concentrated in one or two specific cisternae along the cis-trans axis of the organelle. How such compartmentalized localization of enzymes is achieved and how it contributes to glycosylation are not clear. Here we show that the Golgi matrix protein GRASP55 directs the compartmentalized localization of key enzymes involved in glycosphingolipid (GSL) biosynthesis. GRASP55 acts by binding to these enzymes and preventing their entry to COPI derived retrograde transport vesicles thus concentrating them in the trans-Golgi. In genome edited cells lacking GRASP55 the enzymes relocate to cis-Golgi. Here we evaluated the impact of deleting GRASP55 on sphingolipid composition of HeLa cells by targeted lipid analysis.

ORGANISM(S): Human Homo Sapiens

TISSUE(S): Hela Cells

SUBMITTER: seetharaman parashuraman

PROVIDER: ST001877 | MetabolomicsWorkbench | Sun Jul 18 00:00:00 BST 2021

REPOSITORIES: MetabolomicsWorkbench

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