AN ESSENTIAL ROLE FOR A PHOSPHOLIPID TRANSFER PROTEIN IN YEAST GOLGI FUNCTION
AN ESSENTIAL ROLE FOR A PHOSPHOLIPID TRANSFER PROTEIN IN YEAST GOLGI FUNCTION
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DOI：
10.1038/347561a0
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发表时间：
1990-10-11
期刊：
影响因子：
64.8
通讯作者：
DOWHAN, W
中科院分区：
文献类型：
--
作者：
BANKAITIS, VA;AITKEN, JR;DOWHAN, W
蛋白质通过真核细胞分泌途径的进展涉及到由蛋白质和磷脂组成的大分子结构的连续重排。SEC14p蛋白对于酵母高尔基复合体1的蛋白质运输是必不可少的。对在酵母中编码磷脂酰肌醇/磷脂酰胆碱转移蛋白的SEC14基因2和PIT1基因3的独立鉴定表明，这两个基因是相同的。磷脂转移蛋白是一类广泛存在于真核细胞中的胞质蛋白，其显著特点是能够催化膜之间的磷脂交换。我们在这里证明了SEC14和PIT1基因确实是相同的，并且ASEC 14-1突变体的生长表型延伸到其转移蛋白不能影响磷脂转移蛋白4，5。因此，这些结果首次证实了磷脂转移蛋白的活体功能，即在隔室特异性刺激蛋白质分泌中的作用。
PROGRESSION of proteins through the secretory pathway of eukaryotic cells involves a continuous rearrangement of macromolecular structures made up of proteins and phospholipids. The protein SEC14p is essential for transport of proteins from the yeast Golgi complex1. Independent characterization of theSEC14gene2and thePIT1gene3, which encodes a phosphatidy-linositol/phosphatidylcholine transfer protein in yeast, indicated that these two genes are identical. Phospholipid transfer proteins are a class of cytosolic proteins that are ubiquitous among eukaryotic cells and are distinguished by their ability to catalyse the exchange of phospholipids between membranesin vitro4. We show here that theSEC14andPIT1genes are indeed identical and that the growth phenotype of asec 14-1tsmutant extends to the inability of its transfer protein to effect phospholipid transferin vitro4,5. These results therefore establish for the first time anin vivofunction for a phospholipid transfer protein, namely a role in the compartment-specific stimulation of protein secretion.