Your browser doesn't support javascript.
loading
SLX4IP Antagonizes Promiscuous BLM Activity during ALT Maintenance.
Panier, Stephanie; Maric, Marija; Hewitt, Graeme; Mason-Osann, Emily; Gali, Himabindu; Dai, Anqi; Labadorf, Adam; Guervilly, Jean-Hugues; Ruis, Philip; Segura-Bayona, Sandra; Belan, Ondrej; Marzec, Paulina; Gaillard, Pierre-Henri L; Flynn, Rachel L; Boulton, Simon J.
Afiliação
  • Panier S; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Maric M; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Hewitt G; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Mason-Osann E; Boston University School of Medicine, 72 East Concord Street, Boston, MA 02118, USA.
  • Gali H; Boston University School of Medicine, 72 East Concord Street, Boston, MA 02118, USA.
  • Dai A; Boston University School of Medicine, 72 East Concord Street, Boston, MA 02118, USA.
  • Labadorf A; Boston University School of Medicine, 72 East Concord Street, Boston, MA 02118, USA.
  • Guervilly JH; Centre de Recherche en Cancérologie de Marseille, CRCM, CNRS, Aix Marseille Université, INSERM, Institut Paoli-Calmettes, 27 Boulevard Leï Roure, 13009 Marseille, France.
  • Ruis P; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Segura-Bayona S; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Belan O; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Marzec P; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
  • Gaillard PL; Centre de Recherche en Cancérologie de Marseille, CRCM, CNRS, Aix Marseille Université, INSERM, Institut Paoli-Calmettes, 27 Boulevard Leï Roure, 13009 Marseille, France.
  • Flynn RL; Boston University School of Medicine, 72 East Concord Street, Boston, MA 02118, USA.
  • Boulton SJ; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: simon.boulton@crick.ac.uk.
Mol Cell ; 76(1): 27-43.e11, 2019 10 03.
Article em En | MEDLINE | ID: mdl-31447390
Cancer cells acquire unlimited proliferative capacity by either re-expressing telomerase or inducing alternative lengthening of telomeres (ALT), which relies on telomere recombination. Here, we show that ALT recombination requires coordinate regulation of the SMX and BTR complexes to ensure the appropriate balance of resolution and dissolution activities at recombining telomeres. Critical to this control is SLX4IP, which accumulates at ALT telomeres and interacts with SLX4, XPF, and BLM. Loss of SLX4IP increases ALT-related phenotypes, which is incompatible with cell growth following concomitant loss of SLX4. Inactivation of BLM is sufficient to rescue telomere aggregation and the synthetic growth defect in this context, suggesting that SLX4IP favors SMX-dependent resolution by antagonizing promiscuous BLM activity during ALT recombination. Finally, we show that SLX4IP is inactivated in a subset of ALT-positive osteosarcomas. Collectively, our findings uncover an SLX4IP-dependent regulatory mechanism critical for telomere maintenance in ALT cancer cells.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Neoplasias Ósseas / Proteínas de Transporte / Osteossarcoma / Telômero / RecQ Helicases / Homeostase do Telômero Limite: Animals / Female / Humans Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Neoplasias Ósseas / Proteínas de Transporte / Osteossarcoma / Telômero / RecQ Helicases / Homeostase do Telômero Limite: Animals / Female / Humans Idioma: En Ano de publicação: 2019 Tipo de documento: Article