The Yeast Arf GTPase-activating Protein Age1 Is Regulated by Phospholipase D for Post-Golgi Vesicular Transport

• Published in: The Journal of biological chemistry Vol. 286; no. 7; pp. 5187 - 5196
• Main Authors: Benjamin, Jeremy J.R., Poon, Pak P., Lewis, Stephen M., Auger, Andréanne, Wong, Tania A., Singer, Richard A., Johnston, Gerald C.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 18.02.2011; American Society for Biochemistry and Molecular Biology
• Subjects: ADP-Ribosylation Factors - genetics; ADP-Ribosylation Factors - metabolism; Arf GTPase-activating Protein; Arf1; Biological Transport - physiology; Cell Biology; Diacylglycerol; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Endosomes; G Proteins; Gene Dosage; Golgi; Golgi Apparatus - genetics; Golgi Apparatus - metabolism; GTPase-Activating Proteins - genetics; GTPase-Activating Proteins - metabolism; Membrane Lipids - genetics; Membrane Lipids - metabolism; Membrane Trafficking; Phosphatidylinositol Transfer Protein; Phospholipase D - genetics; Phospholipase D - metabolism; Phospholipid Transfer Proteins - genetics; Phospholipid Transfer Proteins - metabolism; Post-Golgi Transport; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Transport Vesicles - genetics; Transport Vesicles - metabolism; Yeast; Membrane Trafficking; Yeast; Arf1; Arf GTPase-activating Protein; G Proteins; Phosphatidylinositol Transfer Protein; Diacylglycerol; Golgi; Post-Golgi Transport; Endosomes
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M110.185108

Vesicular transport shuttles cargo among intracellular compartments. Several stages of vesicular transport are mediated by the small GTPase Arf, which is controlled in a cycle of GTP binding and hydrolysis by Arf guanine-nucleotide exchange factors and Arf GTPase-activating proteins (ArfGAPs), respectively. In budding yeast the Age2 + Gcs1 ArfGAP pair facilitates post-Golgi transport. We have found the AGE1 gene, encoding another ArfGAP, can in high gene-copy number alleviate the temperature sensitivity of cells carrying mutations affecting the Age2 + Gcs1 ArfGAP pair. Moreover, increased AGE1 gene dosage compensates for the complete absence of the otherwise essential Age2 + Gcs1 ArfGAP pair. Increased dosage of SFH2, encoding a phosphatidylinositol transfer protein, also allows cell growth in the absence of the Age2 + Gcs1 pair, but good growth in this situation requires Age1. The ability of Age1 to overcome the need for Age2 + Gcs1 depends on phospholipase D activity that regulates lipid composition. We show by direct assessment of Age1 ArfGAP activity that Age1 is regulated by lipid composition and can provide ArfGAP function for post-Golgi transport.