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])
ISSN0021-9258
卷号291期号:35页码:18252-18262
发表状态已发表
DOI10.1074/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
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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
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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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