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| Mol. Biol. Cell Aug (2007); 18(8):2912-23 | |
| Nucleoporins prevent DNA damage accumulation by modulating Ulp1-dependent sumoylation processes- | |
| Palancade B, Liu X, Garcia-Rubio M, Aguilera A, Zhao X, Doye V | |
| Institut Curie, Centre de Recherche, and Unite Mixte de Recherche 144 Centre National de la Recherche Scientifique, F-75248 Paris, France- palancad@crie-fr | |
| Abstract: Increasing evidences suggest that nuclear pore complexes -NPCs- control different aspects of nuclear metabolism, including transcription, nuclear organization, and DNA repair- We previously established that the Nup84 complex, a major NPC building block, is part of a genetic network involved in DNA repair- Here, we show that double-strand break -DSB- appearance is linked to a shared function of the Nup84 and the Nup60-Mlp1-2 complexes- Mutants within these complexes exhibit similar genetic interactions and alteration in DNA repair processes as mutants of the SUMO-protease Ulp1- Consistently, these nucleoporins are required for maintenance of proper Ulp1 levels at NPCs and for the establishment of the appropriate sumoylation of several cellular proteins, including the DNA repair factor Yku70- Moreover, restoration of nuclear envelope-associated Ulp1 in nucleoporin mutants reestablishes proper sumoylation patterns and suppresses DSB accumulation and genetic interactions with DNA repair genes- Our results thus provide a molecular mechanism that underlies the connection between NPC and genome stability- | |
| [PUBMED: 17538013] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |