2000 Fiscal Year Final Research Report Summary
Analysis of high molecular proteins localized at the cytoplasmic side of the Golgi apparatus
| Project/Area Number |
11680616
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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 |
Structural biochemistry
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| Research Institution | Fukuoka University |
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Principal Investigator |
MISUMI Yoshio School of Medicine, Fukuoka University, Associate Professor, 医学部, 助教授 (10148877)
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| Project Period (FY) |
1999 – 2000
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| Keywords | Golgi apparatus / Cytoplasmic proteins / Localization signals / Two-Hybrid Screening / Periferal protein |
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| Research Abstract |
Both GCP364/giantin and GCP170 have common structural elements enabling the formation of coiled-coil analogous to the myosin family. It has been proposed that these proteins may involved in protein vesicular transport and the maintenance of the Golgi structure. In this report, to get more information of the biological roles of these Golgi associated proteins, we analyzed the targeting mechanism of GCP372/giantin and GCP170 and searched the interacting proteins with these two proteins. The Golgi targeting and/or retention signal of giantin is in the C-terminal region of cytoplasmic domain of GCP364, and transmembrane domain participates partially as a Golgi retention signal. The importance of cytoplasmic domain in GCP364 for the Golgi localization invoking protein-protein interactions rather than interaction between the TMD and lipid bilayer. We identified a novel Golgi protein, named GCP60 as the interacting protein with GCP364. C-terminal half of GCP60 co-localized with giantin in the Golgi region, however the overexpression of this mutant caused the Golgi fragmentation. These data suggested that GCP60 involved in the maintenance of the Golgi structure through the interaction with giantin. On the other hand, GCP170 has two domains for the Golgi targeting/ or retention. These signals play the independent role for GCP170 localization. First, we screen the interacting protein with GCP170 head region that include the Golgi targeting signal, and identified a novel Golgi protein. These results implies that the many interacting proteins with coiled-coil Golgi proteins makes the protein network surrounding the Golgi apparatus. These protein network including β-spectrin and myosin play the role not only in the maintaining the Golgi structure but also in the vesicular transport to and from the Golgi.
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Research Products
(14 results)
