Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
Trends Cell Biol. 2012 Jan;22(1):1-13. doi: 10.1016/j.tcb.2011.09.001. Epub 2011 Oct 20.
Clathrin-mediated endocytosis in the budding yeast Saccharomyces cerevisiae involves the ordered recruitment, activity and disassembly of nearly 60 proteins at distinct sites on the plasma membrane. Two-color live-cell fluorescence microscopy has proven to be invaluable for in vivo analysis of endocytic proteins: identifying new components, determining the order of protein arrival and dissociation, and revealing even very subtle mutant phenotypes. Yeast genetics and functional genomics facilitate identification of complex interaction networks between endocytic proteins and their regulators. Quantitative datasets produced by these various analyses have made theoretical modeling possible. Here, we discuss recent findings on budding yeast endocytosis that have advanced our knowledge of how -60 endocytic proteins are recruited, perform their functions, are regulated by lipid and protein modifications, and are disassembled, all with remarkable regularity.
网格蛋白介导的内吞作用在出芽酵母酿酒酵母中涉及近 60 种蛋白质在质膜上特定位点的有序募集、活性和组装。双色活细胞荧光显微镜已被证明对于内吞蛋白的体内分析非常有价值：鉴定新的成分，确定蛋白质到达和解离的顺序，并揭示即使是非常微妙的突变表型。酵母遗传学和功能基因组学有助于鉴定内吞蛋白及其调节剂之间的复杂相互作用网络。这些各种分析产生的定量数据集使理论建模成为可能。在这里，我们讨论了关于出芽酵母内吞作用的最新发现，这些发现提高了我们对内吞作用的认识，即-60 种内吞蛋白是如何被招募的，它们如何发挥作用，如何受到脂质和蛋白质修饰的调节，以及如何组装，所有这些都具有显著的规律性。
