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Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions | |
2016-08-26 | |
Source Publication | JOURNAL OF BIOLOGICAL CHEMISTRY
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ISSN | 0021-9258 |
Volume | 291Issue:35Pages:18252-18262 |
Status | 已发表 |
DOI | 10.1074/jbc.M116.737783 |
Abstract | 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. |
Keyword | 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 |
Indexed By | SCI ; EI |
Language | 英语 |
Funding Project | National Natural Science Foundation of China[31570781] |
WOS Research Area | Biochemistry & Molecular Biology |
WOS Subject | Biochemistry & Molecular Biology |
WOS ID | WOS:000383241800018 |
Publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
EI Accession Number | 20163602775230 |
EI Keywords | Cell membranes ; Complex networks ; Mammals ; Mass spectrometry ; Purification |
EI Classification Number | Biological Materials and Tissue Engineering:461.2 ; Computer Systems and Equipment:722 ; Chemistry:801 ; Organic Compounds:804.1 |
WOS Keyword | ER-ASSOCIATED DEGRADATION ; MEMBRANE-PROTEINS ; POLYUBIQUITIN CHAINS ; GP78 ; REQUIRES ; CYTOSOL ; GENERATION ; MORPHOLOGY ; NETWORK ; ENZYMES |
Original Document Type | Article |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1746 |
Collection | 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 |
Corresponding Author | Ye, Yihong; Liu, Yanfen |
Affiliation | 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 |
First Author Affilication | School of Life Science and Technology |
Corresponding Author Affilication | School of Life Science and Technology |
First Signature Affilication | School of Life Science and Technology |
Recommended Citation 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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