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Cited by 90MicroRNA in disease regulationRNA Research and SplicingCancer-related molecular mechanisms research

Genome-wide analysis of YB-1-RNA interactions reveals a novel role of YB-1 in miRNA processing in glioblastoma multiforme

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Wu, Shuai-Lai, Fu, Xing, Huang, Jinyan, Jia, Ting-Ting, Zong, Feng-Yang, Mu, Shi-Rong, Zhu, Hong, Yan, Yong +6 more·2015·Nucleic Acids Research
DOI 10.1093/nar/gkv779PMC PMC4787835
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Abstract

Altered miRNA expression is believed to play a crucial role in a variety of human cancers; however, the mechanisms leading to the dysregulation of miRNA expression remain elusive. In this study, we report that the human Y box-binding protein (YB-1), a major mRNA packaging protein, is a novel modulator of miRNA processing in glioblastoma multiforme (GBM). Using individual nucleotide-resolution crosslinking immunoprecipitation coupled to deep sequencing (iCLIP-seq), we performed the first genome-wide analysis of the in vivo YB-1-RNA interactions and found that YB-1 preferentially recognizes a UYAUC consensus motif and binds to the majority of coding gene transcripts including pre-mRNAs and mature mRNAs. Remarkably, our data show that YB-1 also binds extensively to the terminal loop region of pri-/pre-miR-29b-2 and regulates the biogenesis of miR-29b-2 by blocking the recruitment of microprocessor and Dicer to its precursors. Furthermore, we show that down-regulation of miR-29b by YB-1, which is up-regulated in GBM, is important for cell proliferation. Together, our findings reveal a novel function of YB-1 in regulating non-coding RNA expression, which has important implications in tumorigenesis.

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  • The hypothesis that miR-140-5p-G interferes with conserved RBP pathways is supported by the binding of YBX1 to several miR-140-5p-G target genes in a previously reported YBX1 iCLIP dataset.

    “This hypothesis is supported by the binding of YBX1 to several miR-140-5p-G target genes in a previously reported YBX1 individual nucleotide resolution crosslinking and immunoprecipitation (iCLIP) dataset”

    From Gain-of-function mutation of microRNA-140 in human skeletal dysplasia (2019) · cites this paper as [32]

    The Results ('Genome-wide mapping of YB-1-RNA interactions by iCLIP-seq'; page unavailable) identify this paper as a source of YBX1 iCLIP binding data, and the Discussion says its binding sites are enriched in coding genes. Our copy does not identify several miR-140-5p-G target genes as bound by YBX1, so it supports the dataset attribution but not that specific overlap. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • Ybx1 seCLIP analysis identified a binding motif similar to the Ybx1 binding motif reported previously.

    “Next, Ybx1 seCLIP analysis identified a binding motif similar to the Ybx1 binding motif reported previously30–32”

    From Gain-of-function mutation of microRNA-140 in human skeletal dysplasia (2019) · cites this paper as [32]

  • Computational analysis suggested that the miR-140-5p-G seed in the Ago2 complex and the RBP Ybx1 potentially compete for the same RNA binding sites.

    “Computational analysis suggested that the miR-140-5p-G seed in the Ago2 complex and the RBP, Ybx1 (also known as YB-1), potentially compete for the same RNA binding sites”

    From Gain-of-function mutation of microRNA-140 in human skeletal dysplasia (2019) · cites this paper as [32]

    The Results section describes YB-1 binding to RNA and blocking DGCR8 and Dicer loading onto miR-29b-2 precursors. Our copy does not address computationally predicted competition between YB-1 and an Ago2-bound miR-140-5p-G seed for the same binding sites (searched: miR-140-5p-G, Ago2, and competition). (LLM, conf=0.76)

    Experimental — accuracy not yet measured

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  1. [1]Bartel D.P. MicroRNAs: target recognition and regulatory functions Cell 2009 136 215 233 19167326 PMC3794896
  2. [2]Lee Y. Ahn C. Han J. Choi H. Kim J. Yim J. Lee J. Provost P. Radmark O. Kim S. The nuclear RNase III Drosha initiates microRNA processing Nature 2003 425 415 419 14508493
  3. [3]Han J. Lee Y. Yeom K.H. Kim Y.K. Jin H. Kim V.N. The Drosha-DGCR8 complex in primary microRNA processing Genes Dev. 2004 18 3016 3027 15574589 PMC535913
  4. [4]Landthaler M. Yalcin A. Tuschl T. The human DiGeorge syndrome critical region gene 8 and Its D. melanogaster homolog are required for miRNA biogenesis Curr. Biol. 2004 14 2162 2167 15589161
  5. [5]Lee Y. Kim M. Han J. Yeom K.H. Lee S. Baek S.H. Kim V.N. MicroRNA genes are transcribed by RNA polymerase II EMBO J. 2004 23 4051 4060 15372072 PMC524334
  6. [6]Yi R. Qin Y. Macara I.G. Cullen B.R. Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs Genes Dev. 2003 17 3011 3016 14681208 PMC305252
  7. [7]Bernstein E. Caudy A.A. Hammond S.M. Hannon G.J. Role for a bidentate ribonuclease in the initiation step of RNA interference Nature 2001 409 363 366 11201747
  8. [8]Hammond S.M. Boettcher S. Caudy A.A. Kobayashi R. Hannon G.J. Argonaute2, a link between genetic and biochemical analyses of RNAi Science 2001 293 1146 1150 11498593
  9. [9]Farazi T.A. Hoell J.I. Morozov P. Tuschl T. MicroRNAs in human cancer Adv. Exp. Med. Biol. 2013 774 1 20 23377965 PMC3704221
  10. [11]Kim K.K. Yang Y. Zhu J. Adelstein R.S. Kawamoto S. Rbfox3 controls the biogenesis of a subset of microRNAs Nat. Struct. Mol. Biol. 2014 21 901 910 25240799 PMC4189996
  11. [12]Trabucchi M. Briata P. Garcia-Mayoral M. Haase A.D. Filipowicz W. Ramos A. Gherzi R. Rosenfeld M.G. The RNA-binding protein KSRP promotes the biogenesis of a subset of microRNAs Nature 2009 459 1010 1014 19458619 PMC2768332
  12. [13]Viswanathan S.R. Daley G.Q. Gregory R.I. Selective blockade of microRNA processing by Lin28 Science 2008 320 97 100 18292307 PMC3368499
  13. [14]Wu H. Sun S. Tu K. Gao Y. Xie B. Krainer A.R. Zhu J. A splicing-independent function of SF2/ASF in microRNA processing Mol. Cell 2010 38 67 77 20385090 PMC3395997
  14. [15]Han C. Liu Y. Wan G. Choi H.J. Zhao L. Ivan C. He X. Sood A.K. Zhang X. Lu X. The RNA-binding protein DDX1 promotes primary microRNA maturation and inhibits ovarian tumor progression Cell Rep. 2014 8 1447 1460 25176654 PMC4163106
  15. [16]Eliseeva I.A. Kim E.R. Guryanov S.G. Ovchinnikov L.P. Lyabin D.N. Y-box-binding protein 1 (YB-1) and its functions Biochemistry (Mosc.) 2011 76 1402 1433 22339596
  16. [17]Lyabin D.N. Eliseeva I.A. Ovchinnikov L.P. YB-1 protein: functions and regulation Wiley Interdiscip. Rev. RNA 2014 5 95 110 24217978
  17. [18]Lasham A. Print C.G. Woolley A.G. Dunn S.E. Braithwaite A.W. YB-1: oncoprotein, prognostic marker and therapeutic target Biochem J. 2013 449 11 23 23216250
  18. [19]Kosnopfel C. Sinnberg T. Schittek B. Y-box binding protein 1–a prognostic marker and target in tumour therapy Eur. J. Cell Biol. 2014 93 61 70 24461929
  19. [20]Bergmann S. Royer-Pokora B. Fietze E. Jurchott K. Hildebrandt B. Trost D. Leenders F. Claude J.C. Theuring F. Bargou R. YB-1 provokes breast cancer through the induction of chromosomal instability that emerges from mitotic failure and centrosome amplification Cancer Res. 2005 65 4078 4087 15899797
  20. [21]Bargou R.C. Jurchott K. Wagener C. Bergmann S. Metzner S. Bommert K. Mapara M.Y. Winzer K.J. Dietel M. Dorken B. Nuclear localization and increased levels of transcription factor YB-1 in primary human breast cancers are associated with intrinsic MDR1 gene expression Nat. Med. 1997 3 447 450 9095180
  21. [22]En-Nia A. Yilmaz E. Klinge U. Lovett D.H. Stefanidis I. Mertens P.R. Transcription factor YB-1 mediates DNA polymerase alpha gene expression J. Biol. Chem. 2005 280 7702 7711 15615704
  22. [23]Wu J. Lee C. Yokom D. Jiang H. Cheang M.C. Yorida E. Turbin D. Berquin I.M. Mertens P.R. Iftner T. Disruption of the Y-box binding protein-1 results in suppression of the epidermal growth factor receptor and HER-2 Cancer Res. 2006 66 4872 4879 16651443
  23. [24]Finkbeiner M.R. Astanehe A. To K. Fotovati A. Davies A.H. Zhao Y. Jiang H. Stratford A.L. Shadeo A. Boccaccio C. Profiling YB-1 target genes uncovers a new mechanism for MET receptor regulation in normal and malignant human mammary cells Oncogene 2009 28 1421 1431 19151767
  24. [25]Evdokimova V. Tognon C. Ng T. Ruzanov P. Melnyk N. Fink D. Sorokin A. Ovchinnikov L.P. Davicioni E. Triche T.J. Translational activation of snail1 and other developmentally regulated transcription factors by YB-1 promotes an epithelial-mesenchymal transition Cancer Cell 2009 15 402 415 19411069
  25. [26]El-Naggar A.M. Veinotte C.J. Cheng H. Grunewald T.G. Negri G.L. Somasekharan S.P. Corkery D.P. Tirode F. Mathers J. Khan D. Translational Activation of HIF1alpha by YB-1 Promotes Sarcoma Metastasis Cancer Cell 2015 27 682 697 25965573
  26. [27]Bouvet P. Matsumoto K. Wolffe A.P. Sequence-specific RNA recognition by the Xenopus Y-box proteins. An essential role for the cold shock domain J. Biol. Chem. 1995 270 28297 28303 7499328
  27. [28]Matsumoto K. Meric F. Wolffe A.P. Translational repression dependent on the interaction of the Xenopus Y-box protein FRGY2 with mRNA. Role of the cold shock domain, tail domain, and selective RNA sequence recognition J. Biol. Chem. 1996 271 22706 22712 8798444
  28. [29]Manival X. Ghisolfi-Nieto L. Joseph G. Bouvet P. Erard M. RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins Nucleic Acids Res. 2001 29 2223 2233 11376140 PMC55715
  29. [30]Ise T. Nagatani G. Imamura T. Kato K. Takano H. Nomoto M. Izumi H. Ohmori H. Okamoto T. Ohga T. Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen Cancer Res. 1999 59 342 346 9927044
  30. [31]Okamoto T. Izumi H. Imamura T. Takano H. Ise T. Uchiumi T. Kuwano M. Kohno K. Direct interaction of p53 with the Y-box binding protein, YB-1: a mechanism for regulation of human gene expression Oncogene 2000 19 6194 6202 11175333
  31. [32]Wei W.J. Mu S.R. Heiner M. Fu X. Cao L.J. Gong X.F. Bindereif A. Hui J. YB-1 binds to CAUC motifs and stimulates exon inclusion by enhancing the recruitment of U2AF to weak polypyrimidine tracts Nucleic Acids Res. 2012 40 8622 8636 22730292 PMC3458536
  32. [33]Minich W.B. Maidebura I.P. Ovchinnikov L.P. Purification and characterization of the major 50-kDa repressor protein from cytoplasmic mRNP of rabbit reticulocytes Eur. J. Biochem. 1993 212 633 638 8462540
  33. [34]Evdokimova V.M. Wei C.L. Sitikov A.S. Simonenko P.N. Lazarev O.A. Vasilenko K.S. Ustinov V.A. Hershey J.W. Ovchinnikov L.P. The major protein of messenger ribonucleoprotein particles in somatic cells is a member of the Y-box binding transcription factor family J. Biol. Chem. 1995 270 3186 3192 7852402
  34. [35]Stickeler E. Fraser S.D. Honig A. Chen A.L. Berget S.M. Cooper T.A. The RNA binding protein YB-1 binds A/C-rich exon enhancers and stimulates splicing of the CD44 alternative exon v4 EMBO J. 2001 20 3821 3830 11447123 PMC125550
  35. [36]Skabkina O.V. Lyabin D.N. Skabkin M.A. Ovchinnikov L.P. YB-1 autoregulates translation of its own mRNA at or prior to the step of 40S ribosomal subunit joining Mol. Cell. Biol. 2005 25 3317 3323 15798215 PMC1069629
  36. [37]Konig J. Zarnack K. Rot G. Curk T. Kayikci M. Zupan B. Turner D.J. Luscombe N.M. Ule J. iCLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution Nat. Struct. Mol. Biol. 2010 17 909 915 20601959 PMC3000544
  37. [38]Langmead B. Trapnell C. Pop M. Salzberg S.L. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome Genome Biol. 2009 10 R25 19261174 PMC2690996
  38. [39]Rossbach O. Hung L.H. Khrameeva E. Schreiner S. Konig J. Curk T. Zupan B. Ule J. Gelfand M.S. Bindereif A. Crosslinking-immunoprecipitation (iCLIP) analysis reveals global regulatory roles of hnRNP L RNA Biol. 2014 11 146 155 24526010 PMC3973733
  39. [40]Martin M. Cutadapt removes adapter sequences from high-throughput sequencing reads EMBnet.journal 2011 17 10 12
  40. [41]Quinlan A.R. Hall I.M. BEDTools: a flexible suite of utilities for comparing genomic features Bioinformatics 2010 26 841 842 20110278 PMC2832824
  41. [42]Kozomara A. Griffiths-Jones S. miRBase: annotating high confidence microRNAs using deep sequencing data Nucleic Acids Res. 2014 42 D68 D73 24275495 PMC3965103
  42. [43]Zong F.Y. Fu X. Wei W.J. Luo Y.G. Heiner M. Cao L.J. Fang Z. Fang R. Lu D. Ji H. The RNA-binding protein QKI suppresses cancer-associated aberrant splicing PLoS Genet. 2014 10 e1004289 24722255 PMC3983035
  43. [44]Chen C. Ridzon D.A. Broomer A.J. Zhou Z. Lee D.H. Nguyen J.T. Barbisin M. Xu N.L. Mahuvakar V.R. Andersen M.R. Real-time quantification of microRNAs by stem-loop RT-PCR Nucleic Acids Res. 2005 33 e179 16314309 PMC1292995
  44. [45]Ferre-D'Amare A.R. Doudna J.A. Use of cis- and trans-ribozymes to remove 5′ and 3′ heterogeneities from milligrams of in vitro transcribed RNA Nucleic Acids Res. 1996 24 977 978 8600468 PMC145725
  45. [46]Cancer Genome Atlas Research, N. Comprehensive genomic characterization defines human glioblastoma genes and core pathways Nature 2008 455 1061 1068 18772890 PMC2671642
  46. [47]Cazalla D. Xie M. Steitz J.A. A primate herpesvirus uses the integrator complex to generate viral microRNAs Mol. Cell 2011 43 982 992 21925386 PMC3176678
  47. [48]Gillies J.K. Lorimer I.A. Regulation of p27Kip1 by miRNA 221/222 in glioblastoma Cell Cycle 2007 6 2005 2009 17721077
  48. [49]Medina R. Zaidi S.K. Liu C.G. Stein J.L. van Wijnen A.J. Croce C.M. Stein G.S. MicroRNAs 221 and 222 bypass quiescence and compromise cell survival Cancer Res. 2008 68 2773 2780 18413744 PMC3613850
  49. [50]Quintavalle C. Garofalo M. Zanca C. Romano G. Iaboni M. del Basso De Caro M. Martinez-Montero J.C. Incoronato M. Nuovo G. Croce C.M. miR-221/222 overexpession in human glioblastoma increases invasiveness by targeting the protein phosphate PTPmu Oncogene 2012 31 858 868 21743492 PMC4299860
  50. [51]Zhang J. Han L. Ge Y. Zhou X. Zhang A. Zhang C. Zhong Y. You Y. Pu P. Kang C. miR-221/222 promote malignant progression of glioma through activation of the Akt pathway Int. J. Oncol. 2010 36 913 920 20198336
  51. [52]Chang T.C. Yu D. Lee Y.S. Wentzel E.A. Arking D.E. West K.M. Dang C.V. Thomas-Tikhonenko A. Mendell J.T. Widespread microRNA repression by Myc contributes to tumorigenesis Nat. Genet. 2008 40 43 50 18066065 PMC2628762
  52. [53]Zhang H. Kolb F.A. Brondani V. Billy E. Filipowicz W. Human Dicer preferentially cleaves dsRNAs at their termini without a requirement for ATP EMBO J. 2002 21 5875 5885 12411505 PMC131079
  53. [54]Furnari F.B. Fenton T. Bachoo R.M. Mukasa A. Stommel J.M. Stegh A. Hahn W.C. Ligon K.L. Louis D.N. Brennan C. Malignant astrocytic glioma: genetics, biology, and paths to treatment Genes Dev. 2007 21 2683 2710 17974913
  54. [55]Karsy M. Arslan E. Moy F. Current Progress on Understanding MicroRNAs in Glioblastoma Multiforme Genes Cancer 2012 3 3 15 22893786 PMC3415667
  55. [56]Brower J.V. Clark P.A. Lyon W. Kuo J.S. MicroRNAs in cancer: glioblastoma and glioblastoma cancer stem cells Neurochem Int 2014 77 68 77 24937770 PMC4390175
  56. [57]Skabkin M.A. Evdokimova V. Thomas A.A. Ovchinnikov L.P. The major messenger ribonucleoprotein particle protein p50 (YB-1) promotes nucleic acid strand annealing J. Biol. Chem. 2001 276 44841 44847 11585833
  57. [58]Skabkin M.A. Kiselyova O.I. Chernov K.G. Sorokin A.V. Dubrovin E.V. Yaminsky I.V. Vasiliev V.D. Ovchinnikov L.P. Structural organization of mRNA complexes with major core mRNP protein YB-1 Nucleic Acids Res. 2004 32 5621 5635 15494450 PMC524299
  58. [59]West J.A. Viswanathan S.R. Yabuuchi A. Cunniff K. Takeuchi A. Park I.H. Sero J.E. Zhu H. Perez-Atayde A. Frazier A.L. A role for Lin28 in primordial germ-cell development and germ-cell malignancy Nature 2009 460 909 913 19578360 PMC2729657
  59. [60]Piskounova E. Polytarchou C. Thornton J.E. LaPierre R.J. Pothoulakis C. Hagan J.P. Iliopoulos D. Gregory R.I. Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct mechanisms Cell 2011 147 1066 1079 22118463 PMC3227872
  60. [61]Cho J. Chang H. Kwon S.C. Kim B. Kim Y. Choe J. Ha M. Kim Y.K. Kim V.N. LIN28A is a suppressor of ER-associated translation in embryonic stem cells Cell 2012 151 765 777 23102813
  61. [62]Graf R. Munschauer M. Mastrobuoni G. Mayr F. Heinemann U. Kempa S. Rajewsky N. Landthaler M. Identification of LIN28B-bound mRNAs reveals features of target recognition and regulation RNA Biol. 2013 10 1146 1159 23770886 PMC3849162
  62. [63]Wilbert M.L. Huelga S.C. Kapeli K. Stark T.J. Liang T.Y. Chen S.X. Yan B.Y. Nathanson J.L. Hutt K.R. Lovci M.T. LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance Mol. Cell 2012 48 195 206 22959275 PMC3483422
  63. [64]Nam Y. Chen C. Gregory R.I. Chou J.J. Sliz P. Molecular Basis for Interaction of let-7 MicroRNAs with Lin28 Cell 2011 147 1080 1091 22078496 PMC3277843
  64. [65]Mayr F. Schutz A. Doge N. Heinemann U. The Lin28 cold-shock domain remodels pre-let-7 microRNA Nucleic Acids Res. 2012 40 7492 7506 22570413 PMC3424542
  65. [66]Lightfoot H.L. Bugaut A. Armisen J. Lehrbach N.J. Miska E.A. Balasubramanian S. A LIN28-dependent structural change in pre-let-7g directly inhibits Dicer processing Biochemistry 2011 50 7514 7521 21815640 PMC3361669
  66. [67]Lu Z.H. Books J.T. Ley T.J. YB-1 is important for late-stage embryonic development, optimal cellular stress responses, and the prevention of premature senescence Mol. Cell. Biol. 2005 25 4625 4637 15899865 PMC1140647
  67. [68]Uchiumi T. Fotovati A. Sasaguri T. Shibahara K. Shimada T. Fukuda T. Nakamura T. Izumi H. Tsuzuki T. Kuwano M. YB-1 is important for an early stage embryonic development: neural tube formation and cell proliferation J. Biol. Chem. 2006 281 40440 40449 17082189

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Authors
Wu, S.-L., Fu, X., Huang, J., Jia, T.-T., Zong, F.-Y., Mu, S.-R., Zhu, H., Yan, Y., Qiu, S., Wu, Q., Yan, W., Peng, Y., Chen, J., & Hui, J.
Affiliations
  • Chinese Academy of Sciences (CN)
  • Shanghai Jiao Tong University (CN)
  • Second Military Medical University (CN)
  • Sun Yat-sen University (CN)
  • Second Affiliated Hospital of Zhejiang University (CN)
Corresponding author
Hui, Jingyi
ORCID
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
2015-08-03
Volume
43
Issue
17
Pages
8516-8528
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
DOI
10.1093/nar/gkv779
PMC
PMC4787835
OpenAlex
W1871836978
Cited by
90
References
1
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FWCI
1.98
Type
journal article
Language
en
Open access
Licence
Locations
  • Nucleic Acids Research (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › MicroRNA in disease regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer-related molecular mechanisms research
Keywords
YB-1, Y-box binding protein, microRNA processing, miR-29b, microprocessor complex, Dicer, RNA-binding proteins, glioblastoma, cell proliferation, non-coding RNA regulation
MeSH terms
Binding Sites, Glioblastoma, Humans, Protein Binding, RNA, RNA Processing, Post-Transcriptional, Genome, Human, Gene Expression Regulation, Neoplastic, RNA-Binding Proteins, Sequence Analysis, RNA, Genomics, MicroRNAs, Ribonuclease III, Cell Line, Tumor, Cell Proliferation, Y-Box-Binding Protein 1, HEK293 Cells, High-Throughput Nucleotide Sequencing

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