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ID 50976
フルテキストURL
著者
Koreishi, Mayuko Okayama Univ, Grad Sch Nat Sci & Technol
Yu, Sidney Chinese Univ Hong Kong, Sch Biomed Sci
Oda, Mayumi Okayama Univ, Grad Sch Nat Sci & Technol
Honjo, Yasuko Okayama Univ, Res Core Interdisciplinary Sci RCIS
Satoh, Ayano Okayama Univ, Grad Sch Nat Sci & Technol ORCID Kaken ID publons
抄録
Protein export from the endoplasmic reticulum (ER) is an initial and rate-limiting step of molecular trafficking and secretion. This is mediated by coat protein II (COPII)-coated vesicles, whose formation requires small GTPase Sar1 and 6 Sec proteins including Sec23 and Sec31. Sec31 is a component of the outer layer of COPII coat and has been identified as a phosphoprotein. The initiation and promotion of COPII vesicle formation is regulated by Sar1; however, the mechanism regulating the completion of COPII vesicle formation followed by vesicle release is largely unknown. Hypothesizing that the Sec31 phosphorylation may be such a mechanism, we identified phosphorylation sites in the middle linker region of Sec31. Sec31 phosphorylation appeared to decrease its association with ER membranes and Sec23. Non-phosphorylatable mutant of Sec31 stayed longer at ER exit sites and bound more strongly to Sec23. We also found that CK2 is one of the kinases responsible for Sec31 phosphorylation because CK2 knockdown decreased Sec31 phosphorylation, whereas CK2 overexpression increased Sec31 phosphorylation. Furthermore, CK2 knockdown increased affinity of Sec31 for Sec23 and inhibited ER-to-Golgi trafficking. These results suggest that Sec31 phosphorylation by CK2 controls the duration of COPII vesicle formation, which regulates ER-to-Golgi trafficking.
発行日
2013-01-18
出版物タイトル
PLoS ONE
8巻
1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.0054382
言語
English
論文のバージョン
publisher
査読
有り
DOI
Web of Science KeyUT