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.