Mechanisms governing subcellular localization and function of human RGS2.

摘要: RGS proteins negatively regulate heterotrimeric G at the plasma membrane. RGS2-GFP localizes to nucleus, membrane, and cytoplasm of HEK293 cells. Expression activated G(q) increased RGS2 association with membrane decreased accumulation in suggesting that signal-induced redistribution may function. Thus, we identified characterized a conserved N-terminal domain is necessary sufficient for localization. Mutational biophysical analyses indicated this an amphipathic alpha-helix binds vesicles containing acidic phospholipids. However, targeting function helical did not appear be essential attenuate signaling by G(q). Nevertheless, truncation mutants N terminus essential, potentially serving as scaffold receptors, proteins, or nuclear components. Indeed, directs GFP. Although possesses motif, it lacks import signal enters nucleus passive diffusion. Nuclear does limit its ability signaling, because excluding from was without effect. nonetheless other processes nucleus.