Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions
Zhao, Yupeng1; Zhang, Ting2; Huo, Huanhuan1; Ye, Yihong2; Liu, Yanfen1
2016-08-26
Source PublicationJOURNAL OF BIOLOGICAL CHEMISTRY
ISSN0021-9258
Volume291Issue:35Pages:18252-18262
Status已发表
DOI10.1074/jbc.M116.737783
AbstractThe 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.
Keywordendoplasmic-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 BySCI ; EI
Language英语
Funding ProjectNational Natural Science Foundation of China[31570781]
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000383241800018
PublisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI Accession Number20163602775230
EI KeywordsCell membranes ; Complex networks ; Mammals ; Mass spectrometry ; Purification
EI Classification NumberBiological Materials and Tissue Engineering:461.2 ; Computer Systems and Equipment:722 ; Chemistry:801 ; Organic Compounds:804.1
WOS KeywordER-ASSOCIATED DEGRADATION ; MEMBRANE-PROTEINS ; POLYUBIQUITIN CHAINS ; GP78 ; REQUIRES ; CYTOSOL ; GENERATION ; MORPHOLOGY ; NETWORK ; ENZYMES
Original Document TypeArticle
Citation statistics
Cited Times:13[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttps://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 AuthorYe, Yihong; Liu, Yanfen
Affiliation1.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 AffilicationSchool of Life Science and Technology
Corresponding Author AffilicationSchool of Life Science and Technology
First Signature AffilicationSchool 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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