Development of KSTAR in-vessel components and heating systems

In-vessel components of the Korea Superconducting Tokamak Advanced Research (KSTAR) were developed for 2010 campaign to provide a crucial circumstance for achieving the strongly shaped and diverted plasma. Moreover, the in-vessel components such as limiter, divertor, passive stabilizer, in-vessel control coil (IVCC) system demonstrated good performances satisfying the original design concepts. In addition to the plasma facing components and the IVCC, in-vessel cryo-pump (IVCP) system was also installed to leverage divertor operation. Besides the in-vessel components, there have been substantial progresses in development of the heating and current drive system. The KSTAR heating and current drive system includes all kinds of the major heating systems such as neutral beam injection (NBI), ion cyclotron range of frequency (ICRF), electron cyclotron resonance heating and current drive (ECH and ECCD), lower hybrid current drive (LHCD) systems. As an initial stage for full equipment of the heating systems to total power of 26 MW, several key systems such as 1st NBI (called NBI-1). ICRF, and ECH-assisted startup system successfully demonstrated their excellent feasibilities in the design and performances for dedication to the 2010 campaign. (C) 2011 Elsevier B.V. All rights reserved.X1178sciescopu

Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.

Synaptic-vesicle exocytosis is mediated by the vesicular Ca(2+) sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca(2+) through PIP2. This interaction allows both Ca(2+)-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca(2+) triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca(2+) influx bringing the vesicle membrane close enough for membrane fusion