DICP OpenIR
Exosome cofactor hMTR4 competes with export adaptor ALYREF to ensure balanced nuclear RNA pools for degradation and export
Fan, Jing1; Kuai, Bin1; Wu, Guifen1; Wu, Xudong2; Chi, Binkai1; Wang, Lantian1; Wang, Ke1; Shi, Zhubing1; Zhang, Heng1; Chen, She3; He, Zhisong4; Wang, Siyuan1; Zhou, Zhaocai1; Li, Guohui2; Cheng, Hong1
KeywordAlyref Ars2 Hmtr4 Mrna Export Nuclear Rna Degradation
Source PublicationEMBO JOURNAL
2017-10-02
DOI10.15252/embj.201696139
Volume36Issue:19Pages:2870-2886
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemistry & Molecular Biology ; Cell Biology
WOS Research AreaBiochemistry & Molecular Biology ; Cell Biology
WOS KeywordINTRONLESS MESSENGER-RNAS ; CAP-BINDING COMPLEX ; HUMAN TREX COMPLEX ; SACCHAROMYCES-CEREVISIAE ; POLY(A) POLYMERASE ; TARGETING COMPLEX ; MAMMALIAN-CELLS ; QUALITY-CONTROL ; II TRANSCRIPTS ; RIBOSOMAL-RNA
AbstractThe exosome is a key RNA machine that functions in the degradation of unwanted RNAs. Here, we found that significant fractions of precursors and mature forms of mRNAs and long noncoding RNAs are degraded by the nuclear exosome in normal human cells. Exosome-mediated degradation of these RNAs requires its cofactor hMTR4. Significantly, hMTR4 plays a key role in specifically recruiting the exosome to its targets. Furthermore, we provide several lines of evidence indicating that hMTR4 executes this role by directly competing with the mRNA export adaptor ALYREF for associating with ARS2, a component of the cap-binding complex (CBC), and this competition is critical for determining whether an RNA is degraded or exported to the cytoplasm. Together, our results indicate that the competition between hMTR4 and ALYREF determines exosome recruitment and functions in creating balanced nuclear RNA pools for degradation and export.
Language英语
WOS IDWOS:000412115800007
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/150070
Collection中国科学院大连化学物理研究所
Affiliation1.Univ Chinese Acad Sci, Chinese Acad Sci, State Key Lab Mol Biol,Shanghai Inst Biochem & Ce, Shanghai Key Lab Mol Androl,CAS Ctr Excellence Mo, Shanghai, Peoples R China
2.Chinese Acad Sci, Dalian Inst Chem Phys, Lab Mol Modeling & Design, State Key Lab Mol React Dynam, Dalian, Peoples R China
3.Natl Inst Biol Sci, Beijing, Peoples R China
4.Chinese Acad Sci, Shanghai Inst Biol Sci, CAS MPG Partner Inst Computat Biol, CAS Key Lab Computat Biol, Shanghai, Peoples R China
Recommended Citation
GB/T 7714
Fan, Jing,Kuai, Bin,Wu, Guifen,et al. Exosome cofactor hMTR4 competes with export adaptor ALYREF to ensure balanced nuclear RNA pools for degradation and export[J]. EMBO JOURNAL,2017,36(19):2870-2886.
APA Fan, Jing.,Kuai, Bin.,Wu, Guifen.,Wu, Xudong.,Chi, Binkai.,...&Cheng, Hong.(2017).Exosome cofactor hMTR4 competes with export adaptor ALYREF to ensure balanced nuclear RNA pools for degradation and export.EMBO JOURNAL,36(19),2870-2886.
MLA Fan, Jing,et al."Exosome cofactor hMTR4 competes with export adaptor ALYREF to ensure balanced nuclear RNA pools for degradation and export".EMBO JOURNAL 36.19(2017):2870-2886.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Fan, Jing]'s Articles
[Kuai, Bin]'s Articles
[Wu, Guifen]'s Articles
Baidu academic
Similar articles in Baidu academic
[Fan, Jing]'s Articles
[Kuai, Bin]'s Articles
[Wu, Guifen]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Fan, Jing]'s Articles
[Kuai, Bin]'s Articles
[Wu, Guifen]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.