McGee T P, Skinner H B, Whitters E A, Henry S A, Bankaitis V A
Department of Cell Biology, University of Alabama at Birmingham 35294-0005.
J Cell Biol. 1994 Feb;124(3):273-87. doi: 10.1083/jcb.124.3.273.
SEC14p is required for protein transport from the yeast Golgi complex. We describe a quantitative analysis of yeast bulk membrane and Golgi membrane phospholipid composition under conditions where Golgi secretory function has been uncoupled from its usual SEC14p requirement. The data demonstrate that SEC14p specifically functions to maintain a reduced phosphatidylcholine content in Golgi membranes and indicate that overproduction of SEC14p markedly reduces the apparent rate of phosphatidylcholine biosynthesis via the CDP-choline pathway in vivo. We suggest that SEC14p serves as a sensor of Golgi membrane phospholipid composition through which the activity of the CDP-choline pathway in Golgi membranes is regulated such that a phosphatidylcholine content that is compatible with the essential secretory function of these membranes is maintained.
SEC14p是酵母高尔基体复合体进行蛋白质转运所必需的。我们描述了在高尔基体分泌功能与其通常对SEC14p的需求脱钩的条件下,对酵母整体膜和高尔基体膜磷脂组成的定量分析。数据表明,SEC14p的特定功能是维持高尔基体膜中磷脂酰胆碱含量的降低,并表明SEC14p的过量表达显著降低了体内通过CDP-胆碱途径合成磷脂酰胆碱的表观速率。我们认为,SEC14p作为高尔基体膜磷脂组成的传感器,通过它调节高尔基体膜中CDP-胆碱途径的活性,从而维持与这些膜的基本分泌功能相适应的磷脂酰胆碱含量。