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Showing 1–14 of 14 results
Advanced filters: Author: Karim Mekhail Clear advanced filters

  • Here the authors show that the nucleus undergoes a transient ‘metamorphosis’ within a nuclear–cytoplasmic DNA damage response linked to health and disease. Through this process, the nuclear envelope projects tubules that capture damaged DNA, mediating its repair.

    • Mitra Shokrollahi
    • Mia Stanic
    • Karim Mekhail
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 1319-1330

  • Damaged DNA is often targeted to nuclear pore complexes for repair. Here, the authors show that kinesin-14 mediates this process ensuring error-prone repair, while perinuclear telomere attachment licenses damaged telomeric loci for this repair and kinesin-14 blocks senescence in the absence of telomerase.

    • Daniel K.C. Chung
    • Janet N.Y. Chan
    • Karim Mekhail
    Research
    Nature Communications
    Volume: 6, P: 1-13

  • Non-random positioning of chromosomal domains in the nucleus is a common feature of eukaryotic genomes and has been linked to transcriptional activity, DNA repair, recombination and stability. Nuclear pores and other integral membrane protein complexes are key players in the dynamic organization of the genome in the nucleus.

    • Karim Mekhail
    • Danesh Moazed
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 11, P: 317-328

  • Changes in nuclear and genome organization promote the repair of DNA double-strand breaks and genome stability. Processes that are involved include the modulation of chromatin state, condensates of repair proteins and cytoskeleton reorganization. The reshaping of the nucleus and genome is commonly altered in cancer and during ageing, which could be targeted to provide new therapeutic opportunities.

    • Irene Chiolo
    • Matthias Altmeyer
    • Karim Mekhail
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 26, P: 538-557

  • Genome dynamics allow cells to repair DNA double-strand breaks (DSBs), which are highly toxic DNA lesions. Here the authors reveal that in S. cerevisiae, Rad52 DNA repair proteins assemble in liquid droplets that work with dynamic nuclear microtubules to relocalize lesions to the nuclear periphery for repair.

    • Roxanne Oshidari
    • Richard Huang
    • Karim Mekhail
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-8

  • RNA polymerase II has an unexpected function in the nucleolus, helping to drive the expression of ribosomal RNA and to protect nucleolar structure through a mechanism involving triplex R-loop structures.

    • Karan J. Abraham
    • Negin Khosraviani
    • Karim Mekhail
    Research
    Nature
    Volume: 585, P: 298-302

  • The SMN protein recognizes symmetric dimethylarginine by its Tudor domain, and SMN deficiency leads to spinal muscular atrophy. Here, Liu et al. discover a small molecule that binds to the SMN Tudor domain and disrupts the interaction between SMN and RNA Polymerase II.

    • Yanli Liu
    • Aman Iqbal
    • Jinrong Min
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • Laflamme and Mekhail discuss emerging nuclear roles for LLPS in genome organization, gene expression and DNA repair, highlighting the emerging notion that biomolecular condensates regulate the sequential engagement of molecules in multistep biological processes.

    • Guillaume Laflamme
    • Karim Mekhail
    ReviewsOpen Access
    Communications Biology
    Volume: 3, P: 1-8

  • Lauren Ostrowski, Amanda Hall et al. report a molecular characterization of Pbp1, the yeast ortholog of the neurodegenerative disease-associated human ATXN2. They find that Pbp1 knockout or polyQ expansion compromises rDNA repeat stability via a mechanism linking neurodegenerative protein aggregation and aging.

    • Lauren A. Ostrowski
    • Amanda C. Hall
    • Karim Mekhail
    ResearchOpen Access
    Communications Biology
    Volume: 1, P: 1-17

  • Suppressing the homologous recombination of repetitive DNA sequences is important for maintaining genome stability, and packaging of repeat DNA into silent chromatin was generally thought to protect it from recombination. Yeast ribosomal DNA (rDNA) repetitive sequences are shown to associate with the nuclear periphery via inner nuclear membrane proteins, and this tethering is required for rDNA stability. Sir2-dependent silencing is not sufficient to inhibit rDNA recombination.

    • Karim Mekhail
    • Jan Seebacher
    • Danesh Moazed
    Research
    Nature
    Volume: 456, P: 667-670