Tang Bor Luen, Wang Ya, Ong Yan Shan, Hong Wanjin
Department of Biochemistry, National University of Singapore, 8 Medical Drive, Singapore 117597, Singapore.
Biochim Biophys Acta. 2005 Jul 10;1744(3):293-303. doi: 10.1016/j.bbamcr.2005.02.007. Epub 2005 Mar 17.
First discovered by genetic analysis of yeast secretion mutants, the evolutionarily conserved vesicular coat protein II (COPII) complex is responsible for membrane transport from the endoplasmic reticulum (ER) to the Golgi apparatus. In recent years, extensive efforts in structural, morphological, genetic and molecular analysis have greatly enhanced our understanding of the structural and molecular basis of COPII subunit assembly and selective cargo packaging during ER export. Very recent data have also indicated that a more "classical" picture of vesicle formation from ER exit sites (ERES) followed by their transport to the Golgi is far from accurate. Proteins modulating the function of COPII have also emerged in recent analysis. They either affect COPII-based cargo selection, the formation of vesicle/transport carrier, or subsequent targeting of the transport carrier. Together, elucidation of COPII-mediated ER export has painted a fascinating picture of molecular complexity for an essential process in all eukaryotic cells.
通过对酵母分泌突变体的遗传分析首次发现,进化上保守的囊泡衣被蛋白II(COPII)复合体负责从内质网(ER)到高尔基体的膜运输。近年来,在结构、形态、遗传和分子分析方面的大量努力极大地增进了我们对COPII亚基组装以及内质网输出过程中选择性货物包装的结构和分子基础的理解。最近的数据还表明,从内质网出口位点(ERES)形成囊泡然后将其运输到高尔基体这种更为“经典”的图景远非准确。在最近的分析中还出现了调节COPII功能的蛋白质。它们要么影响基于COPII的货物选择、囊泡/运输载体的形成,要么影响运输载体的后续靶向。总之,对COPII介导的内质网输出的阐明为所有真核细胞中的一个基本过程描绘了一幅迷人的分子复杂性图景。