| Budget Amount *help |
¥4,020,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥420,000)
Fiscal Year 2007: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2006: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Research Abstract |
Golgins are a family of coiled-coil proteins associated with the Golgi apparatus necessary for tethering events in membrane fusion and as structural supports for Golgi cisternae. In the membrane trafficking pathway, long coiled-coil proteins and the multi-subunit complex, are proposed in parallel as candidate tethering factors at each transport step. It is, however, not clear whether two kinds of tethering complexes share a common role and/or a cooperative role in the tethering process. In this project, we examined the interaction of three ER-Golgi golgins (p115, golgin-84 and CASP) and the multi-subunit tethering complex, conserved oligomeric Golgi (COG) complex.
The interaction between p115 and Cog2 was found to be essential for Golgi ribbon reformation after the disruption of the ribbon by p115 knockdown or BFA treatment and recovery by re-expression of p115 or drug wash out respectively. The interaction occurred only in interphase cells and not in mitotic cells. These results strongly suggested that p115 plays an important role in the biogenesis and maintenance of the Golgi by interacting with the COG complex on the cis-Golgi in vesicular trafficking
We previously suggested that integral membrane golgins anchored to the membrane by the COOH-terminal hydrophobic domain, and may be involved in the tethering process of the vesicular transport. We analyzed the interaction of two membrane anchored golgins, such as golgin-84 and CASP, with the COG complex to understand the protein networks around the Golgi apparatus. It demonstrated that the COG complex was co-immunoprecipitate with golgin-84 or CASP. The results suggest that the COG complex interact with two other golgins. Further analysis of interactions between the COG complex and golgins will help in understanding the regulating mechanism of the Golgi integrity.
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