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Intracellular Trafficking Pathway of Yeast Long-chain Base Kinase Lcb4, from Its Synthesis to Its Degradation

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タイトル: Intracellular Trafficking Pathway of Yeast Long-chain Base Kinase Lcb4, from Its Synthesis to Its Degradation
著者: Iwaki, Soichiro 著作を一覧する
Sano, Takamitsu 著作を一覧する
Takagi, Tomoko 著作を一覧する
Osumi, Masako 著作を一覧する
Kihara, Akio 著作を一覧する
Igarashi, Yasuyuki 著作を一覧する
発行日: 2007年 9月28日
出版者: American Society for Biochemistry and Molecular Biology
誌名: Journal of Biological Chemistry
巻: 282
号: 39
開始ページ: 28485
終了ページ: 28492
出版社 DOI: 10.1074/jbc.M701607200
抄録: Sphingoid long-chain base 1-phosphates act as bioactive lipid molecules in eukaryotic cells. In budding yeast, long-chain base 1-phosphates are synthesized mainly by the long-chain base kinase Lcb4. We recently reported that, soon after yeast cells enter into the stationary phase, Lcb4 is rapidly degraded by being delivered to the vacuole in a palmitoylation- and phosphorylation-dependent manner. In this study, we investigated the complete trafficking pathway of Lcb4, from its synthesis to its degradation. After membrane anchoring by palmitoylation at the Golgi apparatus, Lcb4 is delivered to the plasma membrane (PM) through the late Sec pathway and then to the endoplasmic reticulum (ER). The yeast ER consists of a cortical network juxtaposed to the PM (cortical ER) with tubular connections to the nuclear envelope (nuclear ER). Remarkably, the localization of Lcb4 is restricted to the cortical ER. As the cells reach the stationary phase, G1 cell cycle arrest initiates Lcb4 degradation and its delivery to the vacuole via the Golgi apparatus. The protein transport pathway from the PM to the ER found in this study has not been previously reported. We speculate that this novel pathway is mediated by the PM-ER contact.
Rights: Copyright © 2007 by the American Society for Biochemistry and Molecular Biology
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/30180
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 木原 章雄

 

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