Phosphorylation of ULK1 affects autophagosome fusion and links chaperone-mediated autophagy to macroautophagy
文献类型:期刊论文
作者 | Wang, Chenyao2,3; Wang, Huafei3; Zhang, Deyi3; Luo, Wenwen3; Liu, Zhixue3; Liu, Ruilong1; Diao, Lei1; Xu, Daqian6; Liao, Lujian5; Liu, Zhixue4 |
刊名 | NATURE COMMUNICATIONS
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出版日期 | 2018 |
卷号 | 9期号:-页码:3492 |
关键词 | Irrigation Evapotranspiration Crop production Groundwater level Northwest China |
ISSN号 | 2041-1723 |
DOI | 10.1038/s41467-018-05449-1 |
文献子类 | Article |
英文摘要 | The Unc-51 like autophagy activating kinase 1 (ULK1) complex plays a central role in the initiation stage of autophagy. However, the function of ULK1 in the late stage of autophagy is unknown. Here, we report that ULK1, a central kinase of the ULK1 complex involved in autophagy initiation, promotes autophagosome-lysosome fusion. PKC alpha phosphorylates ULK1 and prevents autolysosome formation. PKC alpha phosphorylation of ULK1 does not change its kinase activity; however, it decreases autophagosome-lysosome fusion by reducing the affinity of ULK1 for syntaxin 17 (STX17). Unphosphorylated ULK1 recruited STX17 and increased STX17's affinity towards synaptosomal-associated protein 29 (SNAP29). Additionally, phosphorylation of ULK1 enhances its interaction with heat shock cognate 70 kDa protein (HSC70) and increases its degradation through chaperone-mediated autophagy (CMA). Our study unearths a key mechanism underlying autolysosome formation, a process in which the kinase activity of PKC alpha plays an instrumental role, and reveals the significance of the mutual regulation of macroautophagy and CMA in maintaining the balance of autophagy. |
学科主题 | Science & Technology - Other Topics |
WOS关键词 | KINASE ; COMPLEX ; TARGETS ; CELLS ; ATG14 |
语种 | 英语 |
WOS记录号 | WOS:000442909300016 |
出版者 | NATURE PUBLISHING GROUP |
版本 | 出版稿 |
源URL | [http://202.127.25.144/handle/331004/563] ![]() |
专题 | 中国科学院上海生命科学研究院营养科学研究所 |
作者单位 | 1.Univ Chinese Acad Sci, Shanghai Inst Biol Sci, Chinese Acad Sci, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China; 2.Cleveland Clin, Lerner Res Inst, Dept Immunol, Cleveland, OH 44195 USA; 3.Univ Chinese Acad Sci, Shanghai Inst Biol Sci, Chinese Acad Sci, Inst Nutr Sci,Key Lab Nutr & Metab, Shanghai 200031, Peoples R China; 4.Georgia State Univ, Ctr Mol & Translat Med, Atlanta, GA 30302 USA, 5.East China Normal Univ, Shanghai Key Lab Regulatory Biol, Sch Life Sci, Shanghai 200062, Peoples R China; 6.Univ Texas MD Anderson Canc Ctr, Dept Neuro Oncol, Houston, TX 77030 USA; |
推荐引用方式 GB/T 7714 | Wang, Chenyao,Wang, Huafei,Zhang, Deyi,et al. Phosphorylation of ULK1 affects autophagosome fusion and links chaperone-mediated autophagy to macroautophagy[J]. NATURE COMMUNICATIONS,2018,9(-):3492. |
APA | Wang, Chenyao.,Wang, Huafei.,Zhang, Deyi.,Luo, Wenwen.,Liu, Zhixue.,...&,.(2018).Phosphorylation of ULK1 affects autophagosome fusion and links chaperone-mediated autophagy to macroautophagy.NATURE COMMUNICATIONS,9(-),3492. |
MLA | Wang, Chenyao,et al."Phosphorylation of ULK1 affects autophagosome fusion and links chaperone-mediated autophagy to macroautophagy".NATURE COMMUNICATIONS 9.-(2018):3492. |
入库方式: OAI收割
来源:上海营养与健康研究所
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