OF@TEIN: An OpenFlow-enabled SDN Testbed over International SmartX Rack Sites

In this paper, we will discuss our on-going effort for OF@TEIN SDN(Software-Defined Networking) testbed, which currently spans over Korea and fiveSouth-East Asian (SEA) collaborators with internationally deployed OpenFlowenabledSmartX Racks

iotSilo: The Agent Service Platform Supporting Dynamic Behavior Assembly for Resolving the Heterogeneity of IoT

Although a lot of researchers have painted a rosy picture of Internet of Things (IoT), there have been no widely accepted solution and related standards until now. To achieve the successful realization of IoT, the close collaboration of devices is the primary requisite. However, the heterogeneity of devices such as different hardware or network connectivity prohibits the realization of IoT. In order to overcome the heterogeneity issue, we suggested the agent service platform named iotSilo in which agents can communicate and cooperate on behalf of their devices. With this delegation approach, the iotSilo can support diverse devices without worrying about their differences. In designing an agent, several software design patterns are adopted to enable the agent to assemble behaviors for hiding the heterogeneity of devices. To investigate the effectiveness of the iotSilo, we developed eleven different types of the IoT devices to emulate real world things with Arduino, deployed the devices in both Korea and Japan, and then conducted three experiments

Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation

The human cytomegalovirus glycoprotein US2 induces dislocation of MHC class I heavy chains from the endoplasmic reticulum (ER) into the cytosol and targets them for proteasomal degradation. Signal peptide peptidase (SPP) has been shown to be integral for US2-induced dislocation of MHC class I heavy chains although its mechanism of action remains poorly understood. Here, we show that knockdown of protein disulphide isomerase (PDI) by RNA-mediated interference inhibited the degradation of MHC class I molecules catalysed by US2 but not by its functional homolog US11. Overexpression of the substrate-binding mutant of PDI, but not the catalytically inactive mutant, dominant-negatively inhibited US2-mediated dislocation of MHC class I molecules by preventing their release from US2. Furthermore, PDI associated with SPP independently of US2 and knockdown of PDI inhibited SPP-mediated degradation of CD3δ but not Derlin-1-dependent degradation of CFTR DeltaF508. Together, our data suggest that PDI is a component of the SPP-mediated ER-associated degradation machinery