The late stage of COPI vesicle fission requires shorter forms of phosphatidic acid and diacylglycerol
Journal
Nature Communications
Journal Volume
10
Journal Issue
1
Date Issued
2019
Author(s)
Park S.-Y
Abstract
Studies on vesicle formation by the Coat Protein I (COPI) complex have contributed to a basic understanding of how vesicular transport is initiated. Phosphatidic acid (PA) and diacylglycerol (DAG) have been found previously to be required for the fission stage of COPI vesicle formation. Here, we find that PA with varying lipid geometry can all promote early fission, but only PA with shortened acyl chains promotes late fission. Moreover, diacylglycerol (DAG) acts after PA in late fission, with this role of DAG also requiring shorter acyl chains. Further highlighting the importance of the short-chain lipid geometry for late fission, we find that shorter forms of PA and DAG promote the vesiculation ability of COPI fission factors. These findings advance a general understanding of how lipid geometry contributes to membrane deformation for vesicle fission, and also how proteins and lipids coordinate their actions in driving this process. ? 2019, The Author(s).
Subjects
coat protein complex I; diacylglycerol; lipid; liposome; palmitic acid; phosphatidic acid; small interfering RNA; coat protein complex I; diacylglycerol; phosphatidic acid; chemical compound; geometry; lipid; membrane; protein; Article; cell organelle; cell vacuole; cryoelectron microscopy; endoplasmic reticulum; geometry; Golgi complex; golgi membrane; HeLa cell line; human; human cell; immunofluorescence; lipid composition; lipidomics; molecular dynamics; nonhuman; protein processing; synapse vesicle; transmission electron microscopy; transport assay; vitrification; chemistry; COP-coated vesicle; metabolism; Coat Protein Complex I; COP-Coated Vesicles; Diglycerides; Golgi Apparatus; HeLa Cells; Humans; Phosphatidic Acids
Type
journal article