Cowles C R, Odorizzi G, Payne G S, Emr S D
Division of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California, San Diego 92093-0668, USA.
Cell. 1997 Oct 3;91(1):109-18. doi: 10.1016/s0092-8674(01)80013-1.
Three distinct adaptor protein (AP) complexes involved in protein trafficking have been identified. AP-1 and AP-2 mediate protein sorting at the trans-Golgi network and plasma membrane, respectively, whereas the function of AP-3 has not been defined. A screen for factors specifically involved in transport of alkaline phosphatase (ALP) from the Golgi to the vacuole/lysosome has identified Ap16p and Ap15p of the yeast AP-3 complex. Deletion of each of the four AP-3 subunits results in selective mislocalization of ALP and the vacuolar t-SNARE, Vam3p (but not CPS and CPY), while deletion of AP-1 and AP-2 subunits has no effect on vacuolar protein delivery. This study, therefore, provides evidence that the AP-3 complex functions in cargo-selective protein transport from the Golgi to the vacuole/lysosome.
现已鉴定出三种参与蛋白质运输的不同衔接蛋白(AP)复合物。AP-1和AP-2分别介导反式高尔基体网络和质膜处的蛋白质分选,而AP-3的功能尚未明确。一项针对从高尔基体到液泡/溶酶体的碱性磷酸酶(ALP)运输所涉及的特定因子的筛选,鉴定出了酵母AP-3复合物的Ap16p和Ap15p。四种AP-3亚基中的每一种缺失都会导致ALP和液泡t-SNARE Vam3p(但不是CPS和CPY)的选择性定位错误,而AP-1和AP-2亚基的缺失对液泡蛋白递送没有影响。因此,这项研究提供了证据,表明AP-3复合物在从高尔基体到液泡/溶酶体的货物选择性蛋白质运输中发挥作用。