2010 Fiscal Year Final Research Report
Golgi structure and golgins
Project/Area Number |
20570114
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Fukuoka University |
Principal Investigator |
MISUMI Yoshio Fukuoka University, 医学部, 准教授 (10148877)
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Co-Investigator(Renkei-kenkyūsha) |
SOHDA Miwa 新潟大学, 医歯学系, 助教 (20258528)
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Project Period (FY) |
2008 – 2010
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Keywords | 細胞小器官 / ゴルジ体 / 小胞輸送 / golgin / 局在化 |
Research Abstract |
The coiled-coil Golgi membrane protein golgin-84 functions as a tethering factor for COPI vesicles. Protein interaction analyses have revealed that golgin-84 interacts with another tether, the conserved oligomeric Golgi (COG) complex, through its subunit Cog7. Therefore, we explored the function of golgin-84 as the tether for COPI vesicles of intra-Golgi retrograde traffic. First, glycosylic maturation of both plasma membrane (CD44) and lysosomal (lampl) glycoproteins was distorted in golgin-84 knockdown (KD) cells. The depletion of golgin-84 caused fragmentation of the Golgi with the mislocalization of Golgi resident proteins, resulting in the accumulation of vesicles carrying intra-Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and cis-Golgi membrane protein GPP130. Similar observations were obtained by diminution of the COG complex, suggesting a strong correlation between the two tethers. Indeed, COG complex-dependent (CCD) vesicles that accumulate in Cog3 or Cog7 KD cells carried golgin-84. Surprisingly, the interaction between golgin-84 and another candidate tethering partner CASP (CDP/cut alternatively spliced product) decreased in Cog3 KD cells. These results indicate that golgin-84 on COPI vesicles interact with the COG complex before SNARE assembly, suggesting that the interaction of golgin-84 with COG plays an important role in the tethering process of intra-Golgi retrograde vesicle traffic.
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Research Products
(9 results)
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[Journal Article] YIPFS and YIFIArecycle between the ER and the Golgi apparatus and are involved in the maintenance of the Golgi structure.2008
Author(s)
Yoshida Y, Suzuki K, Yamamoto A, Sakai N, Bando M, Tanimoto K, Yamaguchi Y, Sakaguchi T, Akhter H, Fujii G, Yoshimura SI, Ogata S, Sohda M, Misumi Y, Nakamura N
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Journal Title
Exp Cell Res 314(19)
Pages: 3427-3443
Peer Reviewed
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[Remarks] ホームページ等