Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
CL Baron, V Malhotra - Science, 2002 - science.org
Science, 2002•science.org
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 …
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 …
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.
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