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  1. Article ; Online: GENE REGULATION. Breakers and blockers—miRNAs at work.

    Izaurralde, Elisa

    Science (New York, N.Y.)

    2015  Volume 349, Issue 6246, Page(s) 380–382

    MeSH term(s) Eukaryotic Initiation Factor-4G/metabolism ; Gene Silencing ; Genome, Human ; Humans ; MicroRNAs/physiology ; Protein Biosynthesis/genetics ; RNA Stability ; RNA, Messenger/metabolism
    Chemical Substances Eukaryotic Initiation Factor-4G ; MicroRNAs ; RNA, Messenger
    Language English
    Publishing date 2015-07-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.1260969
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  2. Article ; Online: Crystal structure and functional properties of the human CCR4-CAF1 deadenylase complex.

    Chen, Ying / Khazina, Elena / Izaurralde, Elisa / Weichenrieder, Oliver

    Nucleic acids research

    2021  Volume 49, Issue 11, Page(s) 6489–6510

    Abstract: The CCR4 and CAF1 deadenylases physically interact to form the CCR4-CAF1 complex and function as the catalytic core of the larger CCR4-NOT complex. Together, they are responsible for the eventual removal of the 3'-poly(A) tail from essentially all ... ...

    Abstract The CCR4 and CAF1 deadenylases physically interact to form the CCR4-CAF1 complex and function as the catalytic core of the larger CCR4-NOT complex. Together, they are responsible for the eventual removal of the 3'-poly(A) tail from essentially all cellular mRNAs and consequently play a central role in the posttranscriptional regulation of gene expression. The individual properties of CCR4 and CAF1, however, and their respective contributions in different organisms and cellular environments are incompletely understood. Here, we determined the crystal structure of a human CCR4-CAF1 complex and characterized its enzymatic and substrate recognition properties. The structure reveals specific molecular details affecting RNA binding and hydrolysis, and confirms the CCR4 nuclease domain to be tethered flexibly with a considerable distance between both enzyme active sites. CCR4 and CAF1 sense nucleotide identity on both sides of the 3'-terminal phosphate, efficiently differentiating between single and consecutive non-A residues. In comparison to CCR4, CAF1 emerges as a surprisingly tunable enzyme, highly sensitive to pH, magnesium and zinc ions, and possibly allowing distinct reaction geometries. Our results support a picture of CAF1 as a primordial deadenylase, which gets assisted by CCR4 for better efficiency and by the assembled NOT proteins for selective mRNA targeting and regulation.
    MeSH term(s) Catalytic Domain ; Crystallography, X-Ray ; Exoribonucleases/chemistry ; Exoribonucleases/metabolism ; Fungi/enzymology ; Humans ; Hydrogen-Ion Concentration ; Magnesium ; Models, Molecular ; Protein Conformation ; Protein Domains ; RNA, Messenger/chemistry ; RNA, Messenger/metabolism ; Repressor Proteins/chemistry ; Repressor Proteins/metabolism ; Ribonucleases/chemistry ; Ribonucleases/metabolism ; Zinc
    Chemical Substances RNA, Messenger ; Repressor Proteins ; CNOT7 protein, human (EC 3.1.-) ; Exoribonucleases (EC 3.1.-) ; Ribonucleases (EC 3.1.-) ; cNOT6 protein, human (EC 3.1.-) ; mRNA deadenylase (EC 3.1.-) ; Magnesium (I38ZP9992A) ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2021-05-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkab414
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  3. Article ; Online: A role for eIF4AII in microRNA-mediated mRNA silencing.

    Izaurralde, Elisa

    Nature structural & molecular biology

    2013  Volume 20, Issue 5, Page(s) 543–545

    MeSH term(s) Animals ; Gene Silencing ; Humans ; MicroRNAs/genetics ; MicroRNAs/metabolism ; RNA-Binding Proteins/metabolism
    Chemical Substances MicroRNAs ; RNA-Binding Proteins
    Language English
    Publishing date 2013-05-06
    Publishing country United States
    Document type News ; Comment
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/nsmb.2582
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  4. Article ; Online: Elucidating the temporal order of silencing.

    Izaurralde, Elisa

    EMBO reports

    2012  Volume 13, Issue 8, Page(s) 662–663

    MeSH term(s) Animals ; Drosophila melanogaster/genetics ; Gene Silencing ; Humans ; Models, Genetic ; RNA Stability/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Time Factors ; Zebrafish/genetics
    Chemical Substances RNA, Messenger
    Language English
    Publishing date 2012-06-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.1038/embor.2012.91
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  5. Article: Breakers and blockers—miRNAs at work

    Izaurralde, Elisa

    Science. 2015 July 24, v. 349, no. 6246

    2015  

    Abstract: MicroRNAs (miRNAs) are small, ~22-nucleotide-long noncoding RNAs. They silence the expression of messenger RNAs (mRNAs) containing complementary sequences (1). The human genome encodes ~1500 miRNAs, each with the potential to bind hundreds of different ... ...

    Abstract MicroRNAs (miRNAs) are small, ~22-nucleotide-long noncoding RNAs. They silence the expression of messenger RNAs (mRNAs) containing complementary sequences (1). The human genome encodes ~1500 miRNAs, each with the potential to bind hundreds of different mRNAs (1). miRNAs regulate many biological processes, and the dysregulation of their expression is linked to various human diseases, including cancer (1). To exert their repressive function, miRNAs associate with the Argonaute family of proteins (AGOs) to form the core of miRNA-induced silencing complexes (miRISCs) (1) (see the figure). In animals, miRISCs silence mRNA expression at two levels, by preventing protein production (translation) and inducing mRNA degradation. Over the past decade, progress has been made in our understanding of the mechanism by which miRISCs induce mRNA degradation, but the question of how miRISCs repress translation remains elusive.
    Keywords gene expression ; genome ; human diseases ; humans ; messenger RNA ; microRNA ; neoplasms ; non-coding RNA ; proteins
    Language English
    Dates of publication 2015-0724
    Size p. 380-382.
    Publishing place American Association for the Advancement of Science
    Document type Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.1260969
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  6. Article ; Online: 4E-T-bound mRNAs are stored in a silenced and deadenylated form.

    Räsch, Felix / Weber, Ramona / Izaurralde, Elisa / Igreja, Cátia

    Genes & development

    2020  Volume 34, Issue 11-12, Page(s) 847–860

    Abstract: Human 4E-T is an eIF4E-binding protein (4E-BP) present in processing (P)-bodies that represses translation and regulates decay of mRNAs destabilized by AU-rich elements and microRNAs (miRNAs). However, the underlying regulatory mechanisms are still ... ...

    Abstract Human 4E-T is an eIF4E-binding protein (4E-BP) present in processing (P)-bodies that represses translation and regulates decay of mRNAs destabilized by AU-rich elements and microRNAs (miRNAs). However, the underlying regulatory mechanisms are still unclear. Here, we show that upon mRNA binding 4E-T represses translation and promotes deadenylation via the recruitment of the CCR4-NOT deadenylase complex. The interaction with CCR4-NOT is mediated by previously uncharacterized sites in the middle region of 4E-T. Importantly, mRNA decapping and decay are inhibited by 4E-T and the deadenylated target is stored in a repressed form. Inhibition of mRNA decapping requires the interaction of 4E-T with the cap-binding proteins eIF4E/4EHP. We further show that regulation of decapping by 4E-T participates in mRNA repression by the miRNA effector protein TNRC6B and that 4E-T overexpression interferes with tristetraprolin (TTP)- and NOT1-mediated mRNA decay. Thus, we postulate that 4E-T modulates 5'-to-3' decay by swapping the fate of a deadenylated mRNA from complete degradation to storage. Our results provide insight into the mechanism of mRNA storage that controls localized translation and mRNA stability in P-bodies.
    MeSH term(s) Gene Expression Regulation/genetics ; Gene Silencing/physiology ; Nucleocytoplasmic Transport Proteins/genetics ; Nucleocytoplasmic Transport Proteins/metabolism ; Protein Binding/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Transcription Factors/metabolism
    Chemical Substances EIF4ENIF1 protein, human ; Nucleocytoplasmic Transport Proteins ; RNA, Messenger ; RNA-Binding Proteins ; TNRC6B protein, human ; Transcription Factors
    Language English
    Publishing date 2020-04-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 806684-x
    ISSN 1549-5477 ; 0890-9369
    ISSN (online) 1549-5477
    ISSN 0890-9369
    DOI 10.1101/gad.336073.119
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  7. Article ; Online: Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway.

    Koffa, Maria D / Clements, J Barklie / Izaurralde, Elisa / Wadd, Sarah / Wilson, Stuart A / Mattaj, Iain W / Kuersten, Scott

    The EMBO journal

    2023  Volume 42, Issue 14, Page(s) e114021

    Language English
    Publishing date 2023-06-28
    Publishing country England
    Document type Published Erratum
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2023114021
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  8. Article ; Online: Freedom versus constraint in protein function.

    Izaurralde, Elisa

    Nature reviews. Molecular cell biology

    2009  Volume 10, Issue 6, Page(s) 372

    MeSH term(s) Cytoplasm/chemistry ; Cytoplasm/metabolism ; Exonucleases/metabolism ; RNA, Messenger/metabolism
    Chemical Substances RNA, Messenger ; Exonucleases (EC 3.1.-)
    Language English
    Publishing date 2009-08-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/nrm2697
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  9. Article ; Online: Towards a molecular understanding of microRNA-mediated gene silencing.

    Jonas, Stefanie / Izaurralde, Elisa

    Nature reviews. Genetics

    2015  Volume 16, Issue 7, Page(s) 421–433

    Abstract: MicroRNAs (miRNAs) are a conserved class of small non-coding RNAs that assemble with Argonaute proteins into miRNA-induced silencing complexes (miRISCs) to direct post-transcriptional silencing of complementary mRNA targets. Silencing is accomplished ... ...

    Abstract MicroRNAs (miRNAs) are a conserved class of small non-coding RNAs that assemble with Argonaute proteins into miRNA-induced silencing complexes (miRISCs) to direct post-transcriptional silencing of complementary mRNA targets. Silencing is accomplished through a combination of translational repression and mRNA destabilization, with the latter contributing to most of the steady-state repression in animal cell cultures. Degradation of the mRNA target is initiated by deadenylation, which is followed by decapping and 5'-to-3' exonucleolytic decay. Recent work has enhanced our understanding of the mechanisms of silencing, making it possible to describe in molecular terms a continuum of direct interactions from miRNA target recognition to mRNA deadenylation, decapping and 5'-to-3' degradation. Furthermore, an intricate interplay between translational repression and mRNA degradation is emerging.
    MeSH term(s) Animals ; Gene Silencing ; Humans ; MicroRNAs/metabolism ; Protein Biosynthesis ; RNA Stability
    Chemical Substances MicroRNAs
    Language English
    Publishing date 2015-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2035157-4
    ISSN 1471-0064 ; 1471-0056
    ISSN (online) 1471-0064
    ISSN 1471-0056
    DOI 10.1038/nrg3965
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  10. Article ; Online: Structural and biochemical analysis of a NOT1 MIF4G-like domain of the CCR4-NOT complex.

    Raisch, Tobias / Sandmeir, Felix / Weichenrieder, Oliver / Valkov, Eugene / Izaurralde, Elisa

    Journal of structural biology

    2018  Volume 204, Issue 3, Page(s) 388–395

    Abstract: The CCR4-NOT complex plays a central role in the regulation of gene expression and degradation of messenger RNAs. The multisubunit complex assembles on the NOT1 protein, which acts as a 'scaffold' and is highly conserved in eukaryotes. NOT1 consists of a ...

    Abstract The CCR4-NOT complex plays a central role in the regulation of gene expression and degradation of messenger RNAs. The multisubunit complex assembles on the NOT1 protein, which acts as a 'scaffold' and is highly conserved in eukaryotes. NOT1 consists of a series of helical domains that serve as docking sites for other CCR4-NOT subunits. We describe a crystal structure of a connector domain of NOT1 from the thermophilic fungus Chaetomium thermophilum (Ct). Comparative structural analysis indicates that this domain adopts a MIF4G-like fold and we have termed it the MIF4G-C domain. Solution scattering studies indicate that the human MIF4G-C domain likely adopts a very similar fold to the Ct MIF4G-C. MIF4G domains have been described to mediate interactions with DEAD-box helicases such as DDX6. However, comparison of the interfaces of the MIF4G-C with the MIF4G domain of NOT1 that interacts with DDX6 reveals key structural differences that explain why the MIF4G-C does not bind DDX6. We further show that the human MIF4G-C does not interact stably with other subunits of the CCR4-NOT complex. The structural conservation of the MIF4G-C domain suggests that it may have an important but presently undefined role in the CCR4-NOT complex.
    MeSH term(s) Binding Sites/genetics ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Chaetomium/genetics ; Chaetomium/metabolism ; Crystallography, X-Ray ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Humans ; Models, Molecular ; Protein Binding ; Protein Domains ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances CNOT1 protein, human ; Cell Cycle Proteins ; Fungal Proteins ; Transcription Factors
    Language English
    Publishing date 2018-10-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1032718-6
    ISSN 1095-8657 ; 1047-8477
    ISSN (online) 1095-8657
    ISSN 1047-8477
    DOI 10.1016/j.jsb.2018.10.009
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