1. ALT telomeres get together with nuclear receptors.

    Cell 160(5):811 (2015) PMID 25723159

    Nuclear receptors bind chromosome ends in "alternative lengthening of telomeres" (ALT) cancer cells that maintain their ends by homologous recombination instead of telomerase. Marzec et al. now demonstrate that, in ALT cells, nuclear receptors not only trigger distal chromatin associations to me...
  2. ALT Telomeres Get Together with Nuclear Receptors

    Cell 160(5):811 (2015)

    Nuclear receptors bind chromosome ends in “alternative lengthening of telomeres” (ALT) cancer cells that maintain their ends by homologous recombination instead of telomerase. Marzec et al. now demonstrate that, in ALT cells, nuclear receptors not only trigger distal chromatin associat...
  3. ALT Telomeres Get Together with Nuclear Receptors.

    Cell 160(5):811 (2015) PMID 25723159

    Nuclear receptors bind chromosome ends in "alternative lengthening of telomeres" (ALT) cancer cells that maintain their ends by homologous recombination instead of telomerase. Marzec et al. now demonstrate that, in ALT cells, nuclear receptors not only trigger distal chromatin associations to me...
  4. Telomere functions grounding on TERRA firma.

    Trends in Cell Biology 25(1):29 (2015) PMID 25257515

    Long noncoding telomeric repeat-containing RNAs - TERRAs - are transcribed in a regulated manner from telomeres throughout eukaryotes. TERRA molecules consist of chromosome end-specific subtelomeric sequences and telomeric repeats at their 3' ends. Recent work suggests that TERRA sustains severa...
  5. The shelterin component TPP1 is a binding partner and substrate for the deubiquitinating enzyme USP7.

    Journal of Biological Chemistry 289(41):28595 (2014) PMID 25172512 PMCID PMC4192509

    The telomeric shelterin component TPP1 has critical functions in telomeric protein complex assembly and telomerase recruitment and regulation. Here we identify USP7 as a novel interacting protein of the oligonucleotide/oligosaccharide-binding fold of TPP1, which was previously known to recruit t...
  6. The shelterin component TPP1 is a binding partner and substrate for the deubiquitinating enzyme USP7.

    Journal of Biological Chemistry 289(41):28595 (2014) PMID 25172512 PMCID PMC4192509

    The telomeric shelterin component TPP1 has critical functions in telomeric protein complex assembly and telomerase recruitment and regulation. Here we identify USP7 as a novel interacting protein of the oligonucleotide/oligosaccharide-binding fold of TPP1, which was previously known to recruit t...
  7. The shelterin component TPP1 is a binding partner and substrate for the deubiquitinating enzyme USP7.

    Journal of Biological Chemistry 289(41):28595 (2014) PMID 25172512 PMCID PMC4192509

    The telomeric shelterin component TPP1 has critical functions in telomeric protein complex assembly and telomerase recruitment and regulation. Here we identify USP7 as a novel interacting protein of the oligonucleotide/oligosaccharide-binding fold of TPP1, which was previously known to recruit t...
  8. Telomere functions grounding on TERRA firma

    Trends in Cell Biology 25(1) (2014) PMID 25257515

    • TERRA expression is tightly regulated during the cell cycle and induced upon telomere damage. • Changes in TERRA transcription and abundance may sustain telomere...
  9. Telomere functions grounding on TERRA firma

    Trends in Cell Biology (2014)

    • TERRA expression is tightly regulated during the cell cycle and induced upon telomere damage. • Changes in TERRA transcription and abundance may sustain telomere...
  10. TERRA-reinforced association of LSD1 with MRE11 promotes processing of uncapped telomeres.

    Cell Reports 6(4):765 (2014) PMID 24529708

    Telomeres protect chromosome ends from being recognized as sites of DNA damage. Upon telomere shortening or telomere uncapping induced by loss of telomeric repeat-binding factor 2 (TRF2), telomeres elicit a DNA-damage response leading to cellular senescence. Here, we show that following TRF2 dep...
  11. Functional characterization of the TERRA transcriptome at damaged telomeres.

    Nature Communications 5:5379 (2014) PMID 25359189

    Telomere deprotection occurs during tumorigenesis and aging upon telomere shortening or loss of the telomeric shelterin component TRF2. Deprotected telomeres undergo changes in chromatin structure and elicit a DNA damage response (DDR) that leads to cellular senescence. The telomeric long noncod...
  12. Functional characterization of the TERRA transcriptome at damaged telomeres.

    Nature Communications 5:5379 (2014) PMID 25359189

    Telomere deprotection occurs during tumorigenesis and aging upon telomere shortening or loss of the telomeric shelterin component TRF2. Deprotected telomeres undergo changes in chromatin structure and elicit a DNA damage response (DDR) that leads to cellular senescence. The telomeric long noncod...
  13. Functional characterization of the TERRA transcriptome at damaged telomeres.

    Nature Communications 5:5379 (2014) PMID 25359189 PMCID PMC4264578

    Telomere deprotection occurs during tumorigenesis and aging upon telomere shortening or loss of the telomeric shelterin component TRF2. Deprotected telomeres undergo changes in chromatin structure and elicit a DNA damage response (DDR) that leads to cellular senescence. The telomeric long noncod...
  14. Functional characterization of the TERRA transcriptome at damaged telomeres.

    Nature Communications 5:5379 (2014) PMID 25359189 PMCID PMC4264578

    Telomere deprotection occurs during tumorigenesis and aging upon telomere shortening or loss of the telomeric shelterin component TRF2. Deprotected telomeres undergo changes in chromatin structure and elicit a DNA damage response (DDR) that leads to cellular senescence. The telomeric long noncod...
  15. The THO complex component Thp2 counteracts telomeric R-loops and telomere shortening.

    EMBO Journal 32(21):2861 (2013) PMID 24084588 PMCID PMC3817467

    Telomere maintenance by the conventional DNA replication machinery and telomerase is assisted by specialized DNA helicases, nucleases and telomere binding proteins. Here, we identify the THO components at telomeres and define critical roles of this complex in telomere stability. Deletion of the ...
  16. The THO complex component Thp2 counteracts telomeric R-loops and telomere shortening.

    EMBO Journal 32(21):2861 (2013) PMID 24084588 PMCID PMC3817467

    Telomere maintenance by the conventional DNA replication machinery and telomerase is assisted by specialized DNA helicases, nucleases and telomere binding proteins. Here, we identify the THO components at telomeres and define critical roles of this complex in telomere stability. Deletion of the ...
  17. Molecular basis of telomere syndrome caused by CTC1 mutations.

    Genes & Development 27(19):2099 (2013) PMID 24115768 PMCID PMC3850094

    Mutations in CTC1 lead to the telomere syndromes Coats Plus and dyskeratosis congenita (DC), but the molecular mechanisms involved remain unknown. CTC1 forms with STN1 and TEN1 a trimeric complex termed CST, which binds ssDNA, promotes telomere DNA synthesis, and inhibits telomerase-mediated tel...
  18. A three-state model for the regulation of telomerase by TERRA and hnRNPA1.

    Nucleic Acids Research 41(19):9117 (2013) PMID 23935072 PMCID PMC3799450

    Telomeres, the physical ends of eukaryotic chromosomes, are transcribed into telomeric repeat-containing RNA (TERRA), a large non-coding RNA, which forms an integral part of telomeric heterochromatin. In vitro, naked TERRA molecules are efficient inhibitors of human telomerase, base-pairing via ...
  19. Molecular basis of telomere syndrome caused by CTC1 mutations.

    Genes & Development 27(19):2099 (2013) PMID 24115768 PMCID PMC3850094

    Mutations in CTC1 lead to the telomere syndromes Coats Plus and dyskeratosis congenita (DC), but the molecular mechanisms involved remain unknown. CTC1 forms with STN1 and TEN1 a trimeric complex termed CST, which binds ssDNA, promotes telomere DNA synthesis, and inhibits telomerase-mediated tel...
  20. A three-state model for the regulation of telomerase by TERRA and hnRNPA1.

    Nucleic Acids Research 41(19):9117 (2013) PMID 23935072 PMCID PMC3799450

    Telomeres, the physical ends of eukaryotic chromosomes, are transcribed into telomeric repeat-containing RNA (TERRA), a large non-coding RNA, which forms an integral part of telomeric heterochromatin. In vitro, naked TERRA molecules are efficient inhibitors of human telomerase, base-pairing via ...