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Articles by Gerard L. Brien
A specific form of cPRC1 containing CBX4 is co-opted to mediate oncogenic gene repression in diffuse midline glioma
Endogenous and exogenous immunoprecipitations Harvested cells were washed twice with cold PBS and washed pellets resuspended with Buffer A (25mM HEPES pH 7.6, 5mM MgCl2, 25mM KCl, 0.05mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) NP40, 1mM DTT and 1mM PMSF) and kept on ice for 10 minutes. Samples were centrifuged at 1,500rpm for 10 minutes at 4°C and the supernatant was discarded.
Simultaneous disruption of PRC2 and enhancer function underlies histone H3.3-K27M oncogenic activity in human hindbrain neural stem cells - Nature Genetics
Abstract Driver mutations in genes encoding histone H3 proteins resulting in p.Lys27Met substitutions (H3-K27M) are frequent in pediatric midline brain tumors. However, the precise mechanisms by which H3-K27M causes tumor initiation remain unclear. Here, we use human hindbrain neural stem cells to model the consequences of H3.3-K27M on the epigenomic landscape in a relevant developmental context.
Targeting chromatin complexes in fusion protein-driven malignancies
Abstract Recurrent chromosomal rearrangements leading to the generation of oncogenic fusion proteins are a common feature of many cancers. These aberrations are particularly prevalent in sarcomas and haematopoietic malignancies and frequently involve genes required for chromatin regulation and transcriptional control. In many cases, these fusion proteins are thought to be the primary driver of cancer development, altering chromatin dynamics to initiate oncogenic gene expression programmes.
Exploiting the Epigenome to Control Cancer-Promoting Gene-Expression Programs
Epigenetics refers to heritable traits that are not attributable to changes in DNA sequence. In more specific terms, it can be used to describe how chromatin-associated proteins and reversible chemical modifications of DNA and histone proteins maintain transcriptional programs by regulating chromatin structure (Strahl and Allis, 2000xThe language of covalent histone modifications. Strahl, B.D. and Allis, C.D. Nature.
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