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Title

Understanding the regulation of CtIP roles via its many interactors

AuthorsLópez-Saavedra, Ana ; Huertas Sánchez, Pablo
Issue Date4-Sep-2012
Citation22nd IUBMB - 37th FEBS Congress (2012)
AbstractCtIP is a multifunctional protein involved in several processes through interaction with many different partners. Such functions/ partners include, among others, transcription repression (due to interaction with the transcription repressor CtBP), checkpoint activation (via interaction with MRN complex, the oncogenes Retinoblastoma and Brca1, and the proliferation factor PCNA) and double strand break (DSB) repair by recombination (interaction with Brca1 and the DSB repair factor MRN complex). Some of these interactions seem to be constitutive (CtBP), while others are cell cycle regulated (Rb, Brca1 and MRN). Therefore, CtIP is a key component in the response to DNA DSBs and the preservation of genomic stability that integrate multiple cell-cycle dependent signals. Despite the fact that CtIP has been found interacting with many different partners, it is still unknown if there are additional interactors of CtIP that can regulate its celullar roles. To address this question, we have created a double-tagged (GFP and FLAG) CtIP fusion. Such construct has been integrated in U2OS cells. This cell line can be arrested with double thymidine treatments in the G1/S transition. Upon release from double thymidine, we have isolated proteins from large amounts of cells in different cell cycle phases (G1, S and G2). From these protein samples, CtIP complexes have been immunoprecipitated using an anti-FLAG antibody. After elution with an excess of FLAG peptide, a second immunoprecipitation round using an anti-GFP antibody was performed to ensure maximum purity of the complexes obtained. With this approach, we have isolated new interactors of CtIP.
DescriptionPóster presentado al 22nd IUBMB & 37th FEBS Congress: From Single Molecules to Systems Biology, celebrado en Sevilla (España) del 4 al 9 de septiembre de 2012
URIhttp://hdl.handle.net/10261/123839
Appears in Collections:(CABIMER) Comunicaciones congresos
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