作者: Souhei Sakata , Yasushi Okamura
DOI: 10.1113/JPHYSIOL.2013.263640
关键词:
摘要: Key points The voltage-sensing phosphatase (VSP) consists of the voltage sensor and domain. The movement is coupled to activity. To uncover coupling mechanisms between two domains, we made a mutant VSP. Our analyses showed that this moves in steps. Measurements revealed activity associated with both first second step movements. Results suggest VSP shows graded dependence on extent activation sensor. Abstract The cytoplasmic region, activity. However, its still remain unclear. One possible scenario activated only when fully state. Alternatively, enzymatic single proteins could be distinct states sensor, partial lead phosphatase. To distinguish these possibilities, studied zebrafish VSP, where steps as evidenced by charge movements clamp fluorometry. Measurements toward phosphatidylinositol 4,5-bisphosphate are tuning activities, consistent idea magnitude sensor.