Midori Hosobuchi

TL;DR: In vitro synthesis of endoplasmic reticulum-derived transport vesicles has been reconstituted with washed membranes and three soluble proteins and it is proposed that the coat structures be called COPI and COPII.

TL;DR: In this paper, a chimera consisting of the multiple membrane-spanning domain of yeast hydroxymethylglutaryl CoA reductase fused to yeast histidinol dehydrogenase (HIS4C) is assembled in wild-type or mutant cells such that the His4c protein is oriented to the ER lumen and thus is not available for conversion of cytosolic histidine.

TL;DR: The data suggest that COPI and COPII mediate separate vesicular transport pathways from the ER, which are devoid of endoplasmic reticulum (ER) resident proteins, and each contains targeting proteins necessary for docking at the Golgi complex.

TL;DR: The results indicate that beta-catenin can rescue the dorsal axial structures in a non-cell-autonomous way and without changing the fates of the injected cells, suggesting that cells overexpressing beta-Catenin send a 'dorsal signal' to other cells.

TL;DR: The characterization of SEC21, an essential gene required for protein transport from the endoplasmic reticulum to the Golgi in the yeast Saccharomyces cerevisiae is described and it is demonstrated that a non-clathrin coat protein plays an essential role in intercompartmental transport.