https://scholars.lib.ntu.edu.tw/handle/123456789/416729
標題: | Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p | 作者: | Hsu, J. W. Tang, Pei-Hua Wang, I-Hao Liu, Chia-Lun Chen, Wen-Hui Tsai, Pei-Chin Chen, Kuan-Yu Chen, Kuan-Jung Yu, Chia-Jung Fang-Jen Scott Lee |
關鍵字: | ADP ribosylation factor; ER stress; GTPase; Golgi complex; UPR | 公開日期: | 22-三月-2016 | 出版社: | NATL ACAD SCIENCES | 卷: | 113 | 期: | 12 | 起(迄)頁: | E1683 | 來源出版物: | Proceedings of the National Academy of Sciences of the United States of America | 摘要: | ADP ribosylation factor (Arf) GTPases are key regulators of membrane traffic at the Golgi complex. In yeast, Arf guanine nucleotide-exchange factor (GEF) Syt1p activates Arf-like protein Arl1p, which was accompanied by accumulation of golgin Imh1p at late Golgi, but whether and how this function of Syt1p is regulated remains unclear. Here, we report that the inositol-requiring kinase 1 (Ire1p)-mediated unfolded protein response (UPR) modulated Arl1p activation at late Golgi. Arl1p activation was dependent on both kinase and endo-RNase activities of Ire1p. Moreover, constitutively active transcription factor Hac1p restored the Golgi localization of Arl1p and Imh1p inIRE1-deleted cells. Elucidating the mechanism of Ire1p-Hac1p axis actions, we found that it regulated phosphorylation of Syt1p, which enhances Arl1p activation, recruitment of Imh1p to the Golgi, and Syt1p interaction with Arl1p. Consistent with these findings, the induction of UPR by tunicamycin treatment increases phosphorylation of Syt1p, resulting in Arl1p activation. Thus, these findings clarify how the UPR influences the roles of Syt1p, Arl1p, and Imh1p in Golgi transport. |
URI: | https://api.elsevier.com/content/abstract/scopus_id/84962299844 https://scholars.lib.ntu.edu.tw/handle/123456789/416729 |
ISSN: | 0027-8424 | DOI: | 10.1073/pnas.1518260113 |
顯示於: | 分子醫學研究所 |
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