このエントリーをはてなブックマークに追加
ID 50977
フルテキストURL
著者
Koreishi, Mayuko Okayama Univ, Grad Sch Nat Sci & Technol
Gniadek, Thomas J. Johns Hopkins Univ, Sch Med, Dept Pathol
Yu, Sidney Chinese Univ Hong Kong, Sch Biomed Sci, Shatin
Masuda, Junko NIAID, Mucosal Immun Sect, Lab Host Def
Honjo, Yasuko Okayama Univ, RCIS
Satoh, Ayano Okayama Univ, Grad Sch Nat Sci & Technol 科研費研究者番号
抄録
Golgins are coiled-coil proteins that play a key role in the regulation of Golgi architecture and function. Giantin, the largest golgin in mammals, forms a complex with p115, rab1, GM130, and soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), thereby facilitating vesicle tethering and fusion processes around the Golgi apparatus. Treatment with the microtubule destabilizing drug nocodazole transforms the Golgi ribbon into individual Golgi stacks. Here we show that siRNA-mediated depletion of giantin resulted in more dispersed Golgi stacks after nocodazole treatment than by control treatment, without changing the average cisternal length. Furthermore, depletion of giantin caused an increase in cargo transport that was associated with altered cell surface protein glycosylation. Drosophila S2 cells are known to have dispersed Golgi stacks and no giantin homolog. The exogenous expression of mammalian giantin cDNA in S2 cells resulted in clustered Golgi stacks, similar to the Golgi ribbon in mammalian cells. These results suggest that the spatial organization of the Golgi ribbon is mediated by giantin, which also plays a role in cargo transport and sugar modifications.
発行日
2013-05-21
出版物タイトル
PLoS ONE
8巻
3号
出版者
Public Library Science
ISSN
1932-6203
資料タイプ
学術雑誌論文
オフィシャル URL
http://dx.doi.org/10.1371/journal.pone.0059821
言語
English
論文のバージョン
publisher
査読
有り
DOI
Web of Sience KeyUT