Search

Your search keyword '"Bosch-Presegué, Laia"' showing total 11 results
Start Over Author "Bosch-Presegué, Laia" Search Limiters Peer Reviewed
11 results on '"Bosch-Presegué, Laia"'

3. SIRT1 regulates DNA damage signaling through the PP4 phosphatase complex.

Author

Rasti, George, Becker, Maximilian, Vazquez, Berta N, Espinosa-Alcantud, Maria, Fernández-Duran, Irene, Gámez-García, Andrés, Ianni, Alessandro, Gonzalez, Jessica, Bosch-Presegué, Laia, Marazuela-Duque, Anna, Guitart-Solanes, Anna, Segura-Bayona, Sandra, Bech-Serra, Joan-Josep, Scher, Michael, Serrano, Lourdes, Shankavaram, Uma, Erdjument-Bromage, Hediye, Tempst, Paul, Reinberg, Danny, and Olivella, Mireia

Published
2023
Full Text
View/download PDF

9. SIRT6-dependent cysteine monoubiquitination in the PRE-SET domain of Suv39h1 regulates the NF-κB pathway.

Author

Santos-Barriopedro, Irene, Bosch-Presegué, Laia, Marazuela-Duque, Anna, de la Torre, Carolina, Colomer, Carlota, Vazquez, Berta N., Fuhrmann, Thomas, Martínez-Pastor, Bárbara, Wenfu Lu, Braun, Thomas, Bober, Eva, Jenuwein, Thomas, Serrano, Lourdes, Esteller, Manel, Zhenbang Chen, Barceló-Batllori, Silvia, Mostoslavsky, Raúl, Espinosa, Lluis, and Vaquero, Alejandro

Abstract

Sirtuins are NAD+-dependent deacetylases that facilitate cellular stress response. They include SirT6, which protects genome stability and regulates metabolic homeostasis through gene silencing, and whose loss induces an accelerated aging phenotype directly linked to hyperactivation of the NF-κB pathway. Here we show that SirT6 binds to the H3K9me3- specific histone methyltransferase Suv39h1 and induces monoubiquitination of conserved cysteines in the PRE-SET domain of Suv39h1. Following activation of NF-κB signaling Suv39h1 is released from the IκBα locus, subsequently repressing the NF-κB pathway. We propose that SirT6 attenuates the NF-κB pathway through IκBα upregulation via cysteine monoubiquitination and chromatin eviction of Suv39h1. We suggest a mechanism based on SirT6-mediated enhancement of a negative feedback loop that restricts the NF-κB pathway. [ABSTRACT FROM AUTHOR]

Published
2018
Full Text
View/download PDF

10. Mammalian HP1 Isoforms Have Specific Roles in Heterochromatin Structure and Organization.

Author

Bosch-Presegué, Laia, Raurell-Vila, Helena, Thackray, Joshua K., González, Jessica, Casal, Carmen, Kane-Goldsmith, Noriko, Vizoso, Miguel, Brown, Jeremy P., Gómez, Antonio, Ausió, Juan, Zimmermann, Timo, Esteller, Manel, Schotta, Gunnar, Singh, Prim B., Serrano, Lourdes, and Vaquero, Alejandro

Abstract

HP1 is a structural component of heterochromatin. Mammalian HP1 isoforms HP1α, HP1β, and HP1γ play different roles in genome stability, but their precise role in heterochromatin structure is unclear. Analysis of Hp1α-/-, Hp1β-/-, and Hp1γ-/- MEFs show that HP1 proteins have both redundant and unique functions within pericentric heterochromatin (PCH) and also act globally throughout the genome. HP1α confines H4K20me3 and H3K27me3 to regions within PCH, while its absence results in a global hyper-compaction of chromatin associated with a specific pattern of mitotic defects. In contrast, HP1β is functionally associated with Suv4-20h2 and H4K20me3, and its loss induces global chromatin decompaction and an abnormal enrichment of CTCF in PCH and other genomic regions. Our work provides insight into the roles of HP1 proteins in heterochromatin structure and genome stability. [ABSTRACT FROM AUTHOR]

Published
2017
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results