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Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions | |
2016-08-26 | |
发表期刊 | JOURNAL OF BIOLOGICAL CHEMISTRY (IF:4.0[JCR-2023],4.4[5-Year]) |
ISSN | 0021-9258 |
卷号 | 291期号:35页码:18252-18262 |
发表状态 | 已发表 |
DOI | 10.1074/jbc.M116.737783 |
摘要 | The endoplasmic reticulum (ER) network comprises sheets and tubules that are connected by dynamic three-way junctions. Lunapark (Lnp) localizes to and stabilizes ER three-way junctions by antagonizing the small GTPase Atlastin, but how Lnp shapes the ER network is unclear. Here, we used an affinity purification approach and mass spectrometry to identify Lnp as an interacting partner of the ER protein quality control ubiquitin ligase gp78. Accordingly, Lnp purified from mammalian cells has a ubiquitin ligase activity in vitro. Intriguingly, biochemical analyses show that this activity can be attributed not only to associated ubiquitin ligase, but also to an intrinsic ubiquitin ligase activity borne by Lnp itself. This activity is contained in the N-terminal 45 amino acids of Lnp although this segment does not share homology to any known ubiquitin ligase motifs. Despite its interaction with gp78, Lnp does not seem to have a broad function in degradation of misfolded ER proteins. On the other hand, the N-terminal ubiquitin ligase-bearing motif is required for the ER three-way junction localization of Lnp. Our study identifies a new type of ubiquitin ligase and reveals a potential link between ubiquitin and ER morphology regulation. |
关键词 | endoplasmic-reticulum-associated protein degradation (ERAD) protein misfolding ubiquitin ubiquitin ligase ubiquitin-conjugating enzyme (E2 enzyme) Atlastin ER three-way junction Lunapark Lnp gp78 misfolded |
收录类别 | SCI ; EI |
语种 | 英语 |
资助项目 | National Natural Science Foundation of China[31570781] |
WOS研究方向 | Biochemistry & Molecular Biology |
WOS类目 | Biochemistry & Molecular Biology |
WOS记录号 | WOS:000383241800018 |
出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
EI入藏号 | 20163602775230 |
EI主题词 | Cell membranes ; Complex networks ; Mammals ; Mass spectrometry ; Purification |
EI分类号 | Biological Materials and Tissue Engineering:461.2 ; Computer Systems and Equipment:722 ; Chemistry:801 ; Organic Compounds:804.1 |
WOS关键词 | ER-ASSOCIATED DEGRADATION ; MEMBRANE-PROTEINS ; POLYUBIQUITIN CHAINS ; GP78 ; REQUIRES ; CYTOSOL ; GENERATION ; MORPHOLOGY ; NETWORK ; ENZYMES |
原始文献类型 | Article |
引用统计 | 正在获取...
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文献类型 | 期刊论文 |
条目标识符 | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1746 |
专题 | 生命科学与技术学院 生命科学与技术学院_PI研究组_刘艳芬组 生命科学与技术学院_博士生 |
通讯作者 | Ye, Yihong; Liu, Yanfen |
作者单位 | 1.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China 2.NIDDK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA |
第一作者单位 | 生命科学与技术学院 |
通讯作者单位 | 生命科学与技术学院 |
第一作者的第一单位 | 生命科学与技术学院 |
推荐引用方式 GB/T 7714 | Zhao, Yupeng,Zhang, Ting,Huo, Huanhuan,et al. Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(35):18252-18262. |
APA | Zhao, Yupeng,Zhang, Ting,Huo, Huanhuan,Ye, Yihong,&Liu, Yanfen.(2016).Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions.JOURNAL OF BIOLOGICAL CHEMISTRY,291(35),18252-18262. |
MLA | Zhao, Yupeng,et al."Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions".JOURNAL OF BIOLOGICAL CHEMISTRY 291.35(2016):18252-18262. |
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