Bowers Katherine, Stevens Tom H
Cambridge Institute for Medical Research and Department of Clinical, Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2XY, UK.
Biochim Biophys Acta. 2005 Jul 10;1744(3):438-54. doi: 10.1016/j.bbamcr.2005.04.004.
The late Golgi compartment is a major protein sorting station in the cell. Secreted proteins, cell surface proteins, and proteins destined for endosomes or lysosomes must be sorted from one another at this compartment and targeted to their correct destinations. The molecular details of protein trafficking pathways from the late Golgi to the endosomal system are becoming increasingly well understood due in part to information obtained by genetic analysis of yeast. It is now clear that proteins identified in yeast have functional homologues (orthologues) in higher organisms. We will review the molecular mechanisms of protein targeting from the late Golgi to endosomes and to the vacuole (the equivalent of the mammalian lysosome) of the budding yeast Saccharomyces cerevisiae.
晚期高尔基体区室是细胞中的一个主要蛋白质分选站。分泌蛋白、细胞表面蛋白以及运往内体或溶酶体的蛋白必须在此区室彼此分选,并靶向至其正确的目的地。从晚期高尔基体到内体系统的蛋白质运输途径的分子细节正日益为人所熟知,这部分归功于通过酵母遗传分析获得的信息。现在很清楚,在酵母中鉴定出的蛋白质在高等生物中有功能同源物(直系同源物)。我们将综述酿酒酵母从晚期高尔基体到内体以及到液泡(相当于哺乳动物的溶酶体)的蛋白质靶向的分子机制。