Spatial and temporal regulation of signalling molecules by phosphoinositides

点击翻译按钮获取中文摘要

We developed a new method to quantify and visualize phosphoinositides by the use of Q-dot labeled PH domains which recognize phosphoinositides with high affinity and specificity. By this method, three different phosphoinositides were quantified and visualized simultaneously. We found that FBP17 and CIP4 proteins have F-Bar domains that bind phosphoinositides and deform membranes. F-Bar domain forms a polymerized filament and changes plasma membrane to tube-like structure, resulting in the formation of invaginated pits. We also found a new phosphoinositide binding domain, SYLF domain in SH3YL1, which was involved in the formation of macropinocytosis.