fumonisin-b1 and 1-2-dioctanoylglycerol

fumonisin-b1 has been researched along with 1-2-dioctanoylglycerol* in 1 studies

Other Studies

1 other study(ies) available for fumonisin-b1 and 1-2-dioctanoylglycerol

Article	Year
Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science (New York, N.Y.), 2002, Jan-11, Volume: 295, Issue:5553 Protein kinase D (PKD) is a cytosolic serine-threonine kinase that binds to the trans-Golgi network (TGN) and regulates the fission of transport carriers specifically destined to the cell surface. PKD was found to bind diacylglycerol (DAG), and this binding was necessary for its recruitment to the TGN. Reducing cellular levels of DAG inhibited PKD recruitment and blocked protein transport from the TGN to the cell surface. Thus, a DAG-dependent, PKD-mediated signaling regulates the formation of transport carriers from the TGN in mammalian cells. Topics: Carboxylic Acids; Cell Membrane; Cytosol; Diglycerides; Enzyme Inhibitors; Fumonisins; Golgi Apparatus; HeLa Cells; Humans; Lipid Metabolism; Liposomes; Membrane Glycoproteins; Phosphatidic Acids; Propranolol; Protein Kinase C; Protein Structure, Tertiary; Protein Transport; Recombinant Fusion Proteins; Secretory Vesicles; Signal Transduction; trans-Golgi Network; Vesicular stomatitis Indiana virus; Viral Envelope Proteins	2002

Article

Year

Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane.

Science (New York, N.Y.), 2002, Jan-11, Volume: 295, Issue:5553

Protein kinase D (PKD) is a cytosolic serine-threonine kinase that binds to the trans-Golgi network (TGN) and regulates the fission of transport carriers specifically destined to the cell surface. PKD was found to bind diacylglycerol (DAG), and this binding was necessary for its recruitment to the TGN. Reducing cellular levels of DAG inhibited PKD recruitment and blocked protein transport from the TGN to the cell surface. Thus, a DAG-dependent, PKD-mediated signaling regulates the formation of transport carriers from the TGN in mammalian cells.

Topics: Carboxylic Acids; Cell Membrane; Cytosol; Diglycerides; Enzyme Inhibitors; Fumonisins; Golgi Apparatus; HeLa Cells; Humans; Lipid Metabolism; Liposomes; Membrane Glycoproteins; Phosphatidic Acids; Propranolol; Protein Kinase C; Protein Structure, Tertiary; Protein Transport; Recombinant Fusion Proteins; Secretory Vesicles; Signal Transduction; trans-Golgi Network; Vesicular stomatitis Indiana virus; Viral Envelope Proteins

2002