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  1. Article ; Online: Non-canonical role for the BAF complex subunit DPF3 in mitosis and ciliogenesis.

    Verrillo, Giulia / Obeid, Anna Maria / Genco, Alexia / Scrofani, Jacopo / Orange, François / Hanache, Sarah / Mignon, Julien / Leyder, Tanguy / Michaux, Catherine / Kempeneers, Céline / Bricmont, Noëmie / Herkenne, Stephanie / Vernos, Isabelle / Martin, Maud / Mottet, Denis

    Journal of cell science

    2024  

    Abstract: DPF3, along with other subunits, is a well-known component of the BAF chromatin remodeling complex that plays a key role in regulating chromatin remodeling activity and gene expression. Here, we elucidated a non-canonical localization and role for DPF3. ... ...

    Abstract DPF3, along with other subunits, is a well-known component of the BAF chromatin remodeling complex that plays a key role in regulating chromatin remodeling activity and gene expression. Here, we elucidated a non-canonical localization and role for DPF3. We showed that DPF3 dynamically localizes to the centriolar satellites in interphase and in centrosome, spindle midzone/bridging fiber area and midbodies during mitosis. Loss of DPF3 causes K-fiber instability, unstable kinetochore-microtubules attachment and defects in chromosome alignment, thus resulting in altered mitotic progression, cell death and genomic instability. In addition, we also demonstrated that DPF3 localizes in centriolar satellites at the basis of primary cilia and is required for ciliogenesis by regulating axoneme extension. Together, these findings uncover a moonlighting dual function for DPF3 during mitosis and ciliogenesis.
    Language English
    Publishing date 2024-04-25
    Publishing country England
    Document type Journal Article
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.261744
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: DHX15-independent roles for TFIP11 in U6 snRNA modification, U4/U6.U5 tri-snRNP assembly and pre-mRNA splicing fidelity.

    Duchemin, Amandine / O'Grady, Tina / Hanache, Sarah / Mereau, Agnès / Thiry, Marc / Wacheul, Ludivine / Michaux, Catherine / Perpète, Eric / Hervouet, Eric / Peixoto, Paul / Ernst, Felix G M / Audic, Yann / Dequiedt, Franck / Lafontaine, Denis L J / Mottet, Denis

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 6648

    Abstract: The U6 snRNA, the core catalytic component of the spliceosome, is extensively modified post-transcriptionally, with 2'-O-methylation being most common. However, how U6 2'-O-methylation is regulated remains largely unknown. Here we report that TFIP11, the ...

    Abstract The U6 snRNA, the core catalytic component of the spliceosome, is extensively modified post-transcriptionally, with 2'-O-methylation being most common. However, how U6 2'-O-methylation is regulated remains largely unknown. Here we report that TFIP11, the human homolog of the yeast spliceosome disassembly factor Ntr1, localizes to nucleoli and Cajal Bodies and is essential for the 2'-O-methylation of U6. Mechanistically, we demonstrate that TFIP11 knockdown reduces the association of U6 snRNA with fibrillarin and associated snoRNAs, therefore altering U6 2'-O-methylation. We show U6 snRNA hypomethylation is associated with changes in assembly of the U4/U6.U5 tri-snRNP leading to defects in spliceosome assembly and alterations in splicing fidelity. Strikingly, this function of TFIP11 is independent of the RNA helicase DHX15, its known partner in yeast. In sum, our study demonstrates an unrecognized function for TFIP11 in U6 snRNP modification and U4/U6.U5 tri-snRNP assembly, identifying TFIP11 as a critical spliceosome assembly regulator.
    MeSH term(s) Cell Nucleolus/metabolism ; Cell Survival ; Coiled Bodies/metabolism ; HeLa Cells ; Humans ; Methylation ; Mitosis ; Nuclear Proteins/metabolism ; Nuclear Speckles/metabolism ; Protein Binding ; Protein Stability ; RNA Precursors/metabolism ; RNA Splicing/physiology ; RNA Splicing Factors/genetics ; RNA Splicing Factors/metabolism ; RNA, Small Nuclear/metabolism ; RNA, Small Nucleolar/metabolism ; Ribonucleoprotein, U4-U6 Small Nuclear/metabolism ; Ribonucleoprotein, U5 Small Nuclear/metabolism ; Spliceosomes/metabolism
    Chemical Substances Nuclear Proteins ; RNA Precursors ; RNA Splicing Factors ; RNA, Small Nuclear ; RNA, Small Nucleolar ; Ribonucleoprotein, U4-U6 Small Nuclear ; Ribonucleoprotein, U5 Small Nuclear ; TFIP11 protein, human ; U6 small nuclear RNA ; p80-coilin (136882-81-0)
    Language English
    Publishing date 2021-11-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-021-26932-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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