期刊
DEVELOPMENTAL CELL
卷 45, 期 4, 页码 481-+出版社
CELL PRESS
DOI: 10.1016/j.devcel.2018.04.012
关键词
-
资金
- Wellcome Trust [108042, 100140, 093026, WT 107064]
- MRC Metabolic Disease Unit
- National Institute for Health Research (NIHR) Cambridge Biomedical Research Center
- NIHR Rare Disease Translational Research Collaboration
- BBSRC [BB/M007006/1] Funding Source: UKRI
- MRC [MC_UU_12012/5] Funding Source: UKRI
Cell and organelle membranes consist of a complex mixture of phospholipids (PLs) that determine their size, shape, and function. Phosphatidylcholine ( PC) is the most abundant phospholipid in eukaryotic membranes, yet how cells sense and regulate its levels in vivo remains unclear. Here we show that PCYT1A, the rate-limiting enzyme of PC synthesis, is intranuclear and re-locates to the nuclear membrane in response to the need for membrane PL synthesis in yeast, fly, and mammalian cells. By aligning imaging with lipidomic analysis and data-driven modeling, we demonstrate that yeast PCYT1A membrane association correlates with membrane stored curvature elastic stress estimates. Furthermore, this process occurs inside the nucleus, although nuclear localization signal mutants can compensate for the loss of endogenous PCYT1A in yeast and in fly photoreceptors. These data suggest an ancient mechanism by which nucleoplasmic PCYT1A senses surface PL packing defects on the inner nuclear membrane to control PC homeostasis.
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