Suvorova Elena S, Duden Rainer, Lupashin Vladimir V
Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA.
J Cell Biol. 2002 May 13;157(4):631-43. doi: 10.1083/jcb.200111081.
The Sec34/35 complex was identified as one of the evolutionarily conserved protein complexes that regulates a cis-Golgi step in intracellular vesicular transport. We have identified three new proteins that associate with Sec35p and Sec34p in yeast cytosol. Mutations in these Sec34/35 complex subunits result in defects in basic Golgi functions, including glycosylation of secretory proteins, protein sorting, and retention of Golgi resident proteins. Furthermore, the Sec34/35 complex interacts genetically and physically with the Rab protein Ypt1p, intra-Golgi SNARE molecules, as well as with Golgi vesicle coat complex COPI. We propose that the Sec34/35 protein complex acts as a tether that connects cis-Golgi membranes and COPI-coated, retrogradely targeted intra-Golgi vesicles.
Sec34/35复合体被鉴定为进化保守的蛋白质复合体之一,其在细胞内囊泡运输中调节顺式高尔基体步骤。我们在酵母细胞质中鉴定出三种与Sec35p和Sec34p相关的新蛋白质。这些Sec34/35复合体亚基的突变导致基本高尔基体功能缺陷,包括分泌蛋白的糖基化、蛋白质分选以及高尔基体驻留蛋白的保留。此外,Sec34/35复合体在遗传和物理上与Rab蛋白Ypt1p、高尔基体内部SNARE分子以及高尔基体囊泡包被复合体COPI相互作用。我们提出,Sec34/35蛋白质复合体充当连接顺式高尔基体膜和COPI包被的、逆向靶向的高尔基体内部囊泡的系链。