Article abstract
Nature Cell Biology 7, 225 - 234 (2005)
Published online: 20 February 2005 | doi:10.1038/ncb1221
There is a Corrigendum (April 2005) associated with this Article.
There is a Corrigendum (April 2005) associated with this Article.
Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function
Vladimir Litvak1,3, Nili Dahan1,3, Sreekumar Ramachandran1, Helena Sabanay2 & Sima Lev1
Abstract
The level of diacylglycerol (DAG) in the Golgi apparatus is crucial for protein transport to the plasma membrane. Studies in budding yeast indicate that Sec14p, a phosphatidylinositol (PI)-transfer protein, is involved in regulating DAG homeostasis in the Golgi complex. Here, we show that Nir2, a peripheral Golgi protein containing a PI-transfer domain, is essential for maintaining the structural and functional integrity of the Golgi apparatus in mammalian cells. Depletion of Nir2 by RNAi leads to substantial inhibition of protein transport from the trans-Golgi network to the plasma membrane, and causes a reduction in the DAG level in the Golgi apparatus. Remarkably, inactivation of the cytidine 5'-diphosphate (CDP)-choline pathway for phosphatidylcholine biosynthesis restores both effects. These results indicate that Nir2 is involved in maintaining a critical DAG pool in the Golgi apparatus by regulating its consumption via the CDP-choline pathway, demonstrating the interface between secretion from the Golgi and lipid homeostasis.
- Department of Neurobiology, Weizmann Institute of Science, Rehovot 76100, Israel.
- Electron Microscopy unit, Weizmann Institute of Science, Rehovot 76100, Israel.
- These two authors contributed equally to this work.
Correspondence to: Sima Lev1 e-mail: sima.lev@weizmann.ac.il
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