期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 51, 页码 E7083-E7092出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1521924112
关键词
STIM1; STIM2; ORAI; CRAC channel; store-operated calcium entry
资金
- Waitt Foundation
- W. M. Keck Foundation
- NIH-NCI CCSG [P30 014195]
- NINDS Center Core Grant for Neuroscience Research [P30 NS072031]
- NIH [AI084167, AI040127, GM110397, R01 GM112003]
- Deutsche Forschungsgemeinschaft [QU298/1-1]
- Ruth L. Kirschstein-National Research Service Award Postdoctoral Fellowship
- China Scholarship Council
The stromal interaction molecule (STIM)-ORAI calcium release-activated calcium modulator (ORAI) pathway controls store-dependent calcium entry, a major mechanism of physiological calcium signaling in mammalian cells. The core elements of the pathway are the regulatory protein STIM1, located in the endoplasmic reticulum (ER) membrane, the calcium channel ORAI1 in the plasma membrane, and sites of close contact between the ER and the plasma membrane that permit the two proteins to interact. Research on calcium signaling has centered on STIM1, ORAI1, and a few proteins that directly modulate STIM-ORAI function. However, little is known about proteins that organize ER-plasma membrane junctions for STIM-ORAI-dependent calcium signaling. Here, we report that an ER-resident membrane protein identified in a previous genome-wide RNAi screen, transmembrane protein 110 (TMEM110), regulates the long-term maintenance of ER-plasma membrane junctions and the short-term physiological remodeling of the junctions during store-dependent calcium signaling.
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