A Study on the Contract of Employment about Volunteers: Based on the Legal System and Interpretation of Volunteer Remuneration in France

departmental bulletin pape

The Return of Protectionism to Japan and the United States

PowerPoint presentation which accompanied a discussion with Hisashi Harata, Associate Professor at the University of Tokyo

Research Overview of the Lab. of Molecula Biology, Tohoku University Graduate School of Agricultural Science(Recent Topics of the Agricultunal Biological Science in Tohoku University)

In our laboratory, mainly three different projects described below are now carried out. 1) "Generation and application of the cell membrane permeabilized protein", 2) "Studies on epigenetic regulation of eukaryotic genes through analyses of actin-related proteins" and 3) "Generation of the oxytocin receptor KO (OXTR-/-) mice, and molecular physiological and behavioral analysis of the oxytocin receptor KO (OXTR-/-) mice." In the first project, we generated recombinant Cre protein fused to TAT PTD (protein transduction domain), and the application of this protein into several primary cells prepared from mouse, showed significant recombinase activity. In the second project, we studied epigenetic regulation of eukaryotic genes through analyses of actin-related proteins. In the third project, we obtained several new findings in reproduction, sociosexual behaviors and in physiology of energy/temperature homeostasis of mice as the functions of oxytocin/oxytocin receptor system in vivo, using the oxytocin and its receptor genes deficient (OXT-/- and OXTR-/-) mice. Here we introduce a little about those three projects, respectively

Barriers towards intermodality for pursuing to-work commuters modal shift to bus rapid transit

Institute of Transport and Logistics Studies. Faculty of Economics and Business. The University of Sydne

Molecular mechanisms underlying nucleocytoplasmic shuttling of actinin-4.

In addition to its well-known role as a crosslinker of actin filaments at focal-adhesion sites, actinin-4 is known to be localized to the nucleus. In this study, we reveal the molecular mechanism underlying nuclear localization of actinin-4 and its novel interactions with transcriptional regulators. We found that actinin-4 is imported into the nucleus through the nuclear pore complex in an importin-independent manner and is exported by the chromosome region maintenance-1 (CRM1)-dependent pathway. Nuclear actinin-4 levels were significantly increased in the late G2 phase of the cell cycle and were decreased in the G1 phase, suggesting that active release from the actin cytoskeleton was responsible for increased nuclear actinin-4 in late G2. Nuclear actinin-4 was found to interact with the INO80 chromatin-remodeling complex. It also directs the expression of a subset of cell-cycle-related genes and interacts with the upstream-binding factor (UBF)-dependent rRNA transcriptional machinery in the M phase. These findings provide molecular mechanisms for both nucleocytoplasmic shuttling of proteins that do not contain a nuclear-localization signal and cell-cycle-dependent gene regulation that reflects morphological changes in the cytoskeleton