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Welsby I.,Laboratoire dImmunobiologie | Welsby I.,Free University of Colombia | Hutin D.,Laboratoire dImmunobiologie | Gueydan C.,Laboratoire Of Biologie Moleculaire Du Gene | And 5 more authors.
Journal of Biological Chemistry | Year: 2014

Background: The individual role of members of the poly(ADP-ribose) polymerase family is unclear.Results: PARP12 displays a dual subcellular localization and effector function, controlling both protein translation and NF-κB signaling.Conclusion: PARP12 mediates two important effector mechanisms linked to the establishment of an anti-viral state.Significance: ADP-ribosylation may play an important role in the innate control of microbial infections. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Source

Kharraz Y.,Laboratoire Of Biologie Moleculaire Du Gene | Kharraz Y.,University Pompeu Fabra | Lefort A.,Free University of Colombia | Libert F.,Free University of Colombia | And 3 more authors.
Genomics Data | Year: 2016

TIA-related protein (TIAR) is a RNA-binding protein involved in several steps of gene expression such as RNA splicing Aznarez et al. (2008) [1] and translation Piecyk et al. (2000) [2]. TIAR contains three RNA recognition motifs (RRMs) allowing its interaction with specific sequences localized in the untranslated regions (UTRs) of several mRNAs. In myeloid cells, TIAR has been shown to bind and regulate the translation and stability of various mRNA-encoding proteins important for the inflammatory response, such as TNFα Piecyk et al. (2000), Gueydan et al. (1999) [2,3], Cox-Cok et al. (2003) [4] or IL-Suswam et al. (2005) [5]. Here, we generated two macrophage-like RAW 264.7 cell lines expressing either a tagged full-length TIAR protein or a RRM2-truncated mutant unable to bind RNA with high affinity Dember et al. (1996), Kim et al. (2013) By a combination of RNA-IP and microarray analysis (RIP-chip), we identified mRNAs specifically bound by the full-length protein both in basal conditions and in response to LPS (GSE77577). © 2016. Source

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