期刊
MOLECULAR BIOLOGY OF THE CELL
卷 22, 期 2, 页码 216-229出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E10-04-0317
关键词
-
类别
资金
- National Institutes of Health [GM052549]
The role of specific membrane lipids in transport between endoplasmic reticulum (ER) and Golgi compartments is poorly understood. Using cell-free assays that measure stages in ER-to-Golgi transport, we screened a variety of enzyme inhibitors, lipid-modifying enzymes, and lipid ligands to investigate requirements in yeast. The pleckstrin homology (PH) domain of human Fapp1, which binds phosphatidylinositol-4-phosphate (PI(4) P) specifically, was a strong and specific inhibitor of anterograde transport. Analysis of wild type and mutant PH domain proteins in addition to recombinant versions of the Sac1p phosphoinositide-phosphatase indicated that PI(4) P was required on Golgi membranes for fusion with coat protein complex II (COPII) vesicles. PI(4) P inhibition did not prevent vesicle tethering but significantly reduced formation of soluble n-ethylmaleimide sensitive factor adaptor protein receptor (SNARE) complexes between vesicle and Golgi SNARE proteins. Moreover, semi-intact cell membranes containing elevated levels of the ER-Golgi SNARE proteins and Sly1p were less sensitive to PI(4) P inhibitors. Finally, in vivo analyses of a pik1 mutant strain showed that inhibition of PI(4) P synthesis blocked anterograde transport from the ER to early Golgi compartments. Together, the data presented here indicate that PI(4) P is required for the SNARE-dependent fusion stage of COPII vesicles with the Golgi complex.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据