Springer S, Schekman R
Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720-3202, USA.
Science. 1998 Jul 31;281(5377):698-700. doi: 10.1126/science.281.5377.698.
Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-coated vesicles of secretory and of vesicle targeting (v-SNARE) proteins. Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion. Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p. The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex.
蛋白质从内质网（ER）运输到高尔基体涉及分泌蛋白和囊泡靶向（v-SNARE）蛋白被特异性摄取到包被蛋白复合物II（COPII）包被的囊泡中。在此，两种内质网到高尔基体的v-SNARE蛋白，即Bet1p和Bos1p，被证明以鸟嘌呤核苷酸依赖性方式与COPII包被的组分Sar1p、Sec23p和Sec24p特异性相互作用。其他v-SNARE蛋白，Sec22p和Ykt6p，可能与COPII包被的相互作用较弱，或者通过与Bet1p或Bos1p结合而间接相互作用。数据表明跨膜蛋白可通过与包被蛋白的直接相互作用被摄取到COPII囊泡中，并可能在COPII包被复合物的组装中发挥结构作用。
