2004 Fiscal Year Final Research Report Summary
The analysis of the transport vesicle tethering mechanism in the Golgi apparatus.
| Project/Area Number |
15570128
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Fukuoka University |
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Principal Investigator |
MIWA Sohda Fukuoka University, School of Medicine, Assistant Professor, 医学部, 助手 (20258528)
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| Project Period (FY) |
2003 – 2004
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| Keywords | Golgi apparatus / vesicular transport |
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| Research Abstract |
Protein transport between organelle is mediated by transport vesicles. Targeting of transport vesicles to the correct membrane compartment is multi-layered processes consist of tethering, docking and fusion. High fidelity vesicle transfer is essential for the establishment and maintenance of organelle structure and biosynthetic transport.
Tethering is the first step of contact between a vesicle and its target membrane prior to fusion. Recently many factors in this step have been identified. Proteins proposed as candidate tethering factors fall into two general classes; one belongs to a class of long coiled-coil proteins, and the other is multi-subunit complexes. In the intra-Golgi membrane transport process, the former is the p 1 15/GM 130/giantin (called golgins) complex and the latter is the conserved oligomeric Golgi (COG) complex. p115 tethers COPI vesicles to the Golgi membrane by interaction with two other golgins giantin on the vesicles and GM130 on the Golgi membrane. The COG complex contains eight subunits (COG 1-8). Cells expressing mutant COG1 or COG2 show abnormal glycosylation. These two sets of complex are proposed in parallel as candidate tethering factors; therefore it is remain to resolve whether they act separately or cooperatively.
In this study I have demonstrated two sets of complex interact each other. COG2 was identified as a p 115 binding protein by the yeast two-hybrid screening. The interaction of p 115 and COG2 was showed both in vitro and in vivo.The expression of p115 lacking COG2 binding domain-in p115-depleted cells resulted in the formation of an irregular Golgi structure consist of converged tubular and vesicular structures in the perinuclear area. These results suggest that the interaction between p 115 and the COG complex is Essential for normal Golgi ribbon formation.
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Research Products
(2 results)
