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Recently, technological innovation is a critical element for a country's economic growth. Also, the role of university transfers from educational provider to “entrepreneurial university”. Thus, the university starts to play the role as one to make technology commercialization in terms of technology transfer. Most of the previous research focuses on the economic and social perspective to analyze the contribution of technology commercialization. Due to many key stakeholders and influential factors involving in the whole process, which were seldom taken into account in the research, this research tries to analyze the process from the service design perspective. The aim of the research is to figure out the main factors to change the technology transfer process from passive to active. During observation and interview, the authors discovered that in addition to improving the process by changing the original one, other influential factors such as the employees' interests, regulations of technology transfer, and executors' mindsets of achieving the goals are essential to promote transferring technology to an ideal status and level.

The molecular mechanisms that temporally and spatially coordinate cell morphogenesis with the cell cycle remain poorly understood. Here we describe the characterization of fission yeast Mob2p, a novel protein required for regulating cell polarity and cell cycle control. Deletion of mob2 is lethal and causes cells to become spherical, with depolarized actin and microtubule cytoskeletons. A decrease in Mob2p protein level results in a defect in the activation of bipolar growth. This phenotype is identical to that of mutants defective in the orb6 protein kinase gene, and we find that Mob2p physically interacts with Orb6p. In addition, overexpression of Mob2p, like that of Orb6p, results in a delay in the onset of mitosis. Mob2p localizes to the cell periphery and cytoplasm throughout the cell cycle and to the division site during late anaphase and telophase. Mob2p is unable to localize to the cell middle in mutants defective in actomyosin ring and septum formation. Our results suggest that Mob2p, along with Orb6p, is required for coordinating polarized cell growth during interphase with the onset of mitosis.

The Sid2p-Mob1p kinase complex is an important component of the septation initiation network (SIN) in the fission yeast Schizosaccharomyces pombe. However, regulation of this complex is still elusive. Here we show that Mob1p is required not only for the subcellular localization of Sid2p but also for its kinase activity. We identified a region at the amino terminus of Sid2p that is required for Mob1p binding and spindle pole body (SPB) localization. Deletion of this region abolishes Mob1p binding and diminishes SPB localization, whereas this region alone is sufficient to associate with Mob1p and SPBs. We further show that a similar region of the N terminus of the Sid2p-related protein kinase Orb6p binds to the Mob1p-related protein Mob2p, suggesting that this may be a conserved mode of interaction for this family of kinases. Phosphorylation of Ser402 and especially Thr578 is important for Sid2p function. Sid2p with a mutation of Thr578 to Ala (T578A) can no longer rescue sid2-250 mutant cells, and this results in reduction of Mob1p binding. Sid2p mutants mimicking phosphorylation at this site (T578D and T578E) can rescue sid2-250 cells, enhance Sid2p kinase activity, and partially rescue growth defects of upstream sin mutants. Interestingly, Sid2p, but not Mob1p, is self-associated. Our experiments suggest that self-associated Sid2p is inactive. This self-association is mediated by a region that overlaps with Mob1p and SPB binding sites. Overexpression of Mob1p is able to disrupt the self-association of Sid2p. Taken together, our results suggest that Sid2p kinase may utilize multiple modes of regulation including self-association, Mob1p binding, and phosphorylation to achieve its full activity at an appropriate time and place in the cell.

Faithful actomyosin ring assembly is pivotal for successful cell division. The mechanisms by which the actomyosin ring is assembled at the correct time and place remain unclear. Recent studies in fission yeast have shown that a myosin II-containing spot may be a novel progenitor structure essential for actomyosin ring assembly.

In fission yeast, Scd1/Ral1 is a putative guanine nucleotide exchange factor for Cdc42sp and also acts as a Ras1 effector necessary for the regulation of cytoskeleton organization. In this study, we have characterized a protein, Moe1, that binds directly to Scd1. A moe1 null (Δ) mutant exhibits numerous phenotypes indicative of abnormal microtubule functioning, including an abnormality in the spindle. moe1 Δ mutants are resistant to microtubule destabilizing agents; moreover, moe1 Δ rescued the growth defects of tubulin mutants containing unstable microtubules. These results suggest that Moe1 induces instability in microtubules. Biochemical and subcellular localization studies suggest that Moe1 and Scd1 colocalize in the nucleus. Furthermore, loss of function in Scd1 or Ras1 also induced abnormality in the spindle and is synthetically lethal with moe1 Δ producing cells that lack a detectable spindle. These data demonstrate that Moe1 is a component of the Ras1 pathway necessary for proper spindle formation in the nucleus. Human and nematode Moe1 both can substitute for yeast Moe1, indicating that the function of Moe1 in spindle formation has been conserved substantially during evolution.

Okadaic acid (OA), a potent inhibitor of protein phosphatases 1 and 2A, has been widely used as a tool for unravelling the regulation of cellular metabolic processes involving protein phosphorylation/dephosphorylation. It has recently been found that OA can induce reversible hyperphosphorylation of vimentin and reorganization of intermediate filaments [Lee et al., J. Cell. Biochem. 49: 378–393, 1992]. We report here that OA specifically induced the synthesis of a 78-kDa protein, which was identified as the 78-kDa glucose-regulated protein (GRP78) by two-dimensional sodium dodecylsulfate-polyacrylamide gel electrophoresis and peptide mapping. The induction of GRP78 by OA was dose-dependent and reversible. For 7 h treatments, GRP78 synthesis was initially enhanced under 50 nM OA and became the highest (about 6-fold) under 200 nM OA. Meanwhile, under 200 nM OA, GRP78 synthesis was initially enhanced after 4 h and reached its maximal level (about 8-fold) after 15 h of treatment. Subsequently, upon removal of OA, the level of OA-induced GRP78 was reduced to basal level after 12 h of recovery. Induction of GRP78 synthesis by OA was abolished in cells pretreated with actinomycin D and cycloheximide, indicating that it was regulated at the transcriptional level and its induction required de novo protein synthesis. Furthermore, OA suppressed protein glycosylation, and the result lent support to the hypothesis that suppression of protein glycosylation may correlate with induction of GRP78 synthesis. © 1993 Wiley-Liss, Inc.

A great deal is now known about how cells regulate entry into mitosis, but only recently have the mechanisms controlling exit from mitosis and cytokinesis begun to be revealed. In the budding yeast Saccharomyces cerevisiae , Mob1p interacts with the Dbf2p kinase and cells containing mutations in these genes arrest in late anaphase [1,2]. Proteins related to Mob1p are present in both plants and animals, but information about Mob1p function has been obtained only from budding yeast. Here, we describe the identification and characterization of Mob1p from Schizosaccharomyces pombe . Mob1p associates with the Sid2p kinase and like Sid2p, Mob1p is required for the initiation of cytokinesis, but not for mitotic exit. Mob1p localizes to the spindle pole body (SPB) and to the cell-division site during cell division, suggesting that it might be involved in transducing the signal to initiate cell division from the SPB to the division site. Mob1p is required for Sid2p localization, and Mob1p localization requires the function of the cdc7, cdc11, cdc14, spg1, sid1, sid2, and sid4 genes, suggesting that together with Sid2p, Mob1p functions at the end of the signaling cascade required to regulate the onset of cytokinesis at the end of mitosis.