Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 51, Pages E7083-E7092Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1521924112
Keywords
STIM1; STIM2; ORAI; CRAC channel; store-operated calcium entry
Categories
Funding
- 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
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available