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Bromodomain and PHD finger-containing protein 1 (BRPF1) is an essential epigenetic regulator and plays a key role in post-translational modification of histones. It is a chromatin reader that recognizes acetylated histones and interacts with the paralogous lysine acetyltransferases KAT6A and KAT6B to promote histone acetylation and related acylations, such as propionylation, at lysine 23 of histone H3, thereby influencing gene expression and regulating developmental programs. BRPF1 contributes to a variety of cellular processes such as cell cycle progression, cell proliferation, cell differentiation, and responses to cellular stresses, including DNA damage. Moreover, BRPF1 is implicated in hematopoiesis, embryonic development, skeletal development, neurodevelopment, neurogenesis, learning, and memory. BRPF1 gene knockout in mice leads to severe bone marrow failure, anemia, and eventual death in a few weeks after birth. This review provides a brief overview of BRPF1 and its contribution to the molecular structure and biological functions of KAT6A and KAT6B complexes. We will explore the emerging evidence linking BRPF1 dysfunction to human diseases, particularly cancer and abnormal neurodevelopment, to highlight promising therapeutic opportunities for treating associated pathology.
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http://dx.doi.org/10.1007/978-3-031-91459-1_15 | DOI Listing |
PLoS Pathog
September 2025
Institute of Medical Virology, University of Zurich, Zurich, Switzerland.
SUMO-modified Tripartite Motif Protein 28 (TRIM28; KAP1) plays a crucial role in repressing endogenous retroelement (ERE) transcription. We previously provided evidence that loss of SUMO-modified TRIM28 triggered by influenza A virus (IAV) infection promotes activation of host antiviral immunity via a mechanism involving derepression of EREs and production of immunostimulatory RNAs. While the IAV NS1 protein might limit consequences of such activation via its dsRNA-binding activity, we hypothesized that other human pathogenic viruses could have evolved more direct strategies to counteract this potential ERE-based defense system.
View Article and Find Full Text PDFBiochemistry
August 2025
Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States.
Histone variant H2A.Z has been increasingly associated with cancer progression, including cancers characterized by the dysregulated function of the epigenetic reader protein BPTF (bromodomain and PHD finger containing transcription factor). Despite this association, a direct interaction between acetylated H2A.
View Article and Find Full Text PDFGenome Biol
August 2025
State Key Laboratory of Metabolism and Regulation in Complex Organisms, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, 115 DongHu Road, Research Building III, Room 404, Wuchang District, Wuhan, 430071, China.
Background: KAT6A-CBP (K/C) and KAT6A-P300 (K/P) fusions are recurrent genetic alterations in acute myeloid leukemia (AML) associated with poor prognosis. Despite their strong oncogenic potential, the mechanisms underlying their genomic targeting and leukemogenic function remain unclear. A major challenge has been their large size, which has impeded preclinical model development and mechanistic studies.
View Article and Find Full Text PDFbioRxiv
June 2025
Departments of Physics and Biology, Illinois Institute of Technology, Chicago, USA.
Many transcription factors regulate DNA accessibility and gene expression by recognizing post-translational modifications on histone tails within nucleosomes. These interactions are often studied using short peptide mimics of histone tails, which may overlook conformational changes that occur in the full nucleosomal context. Here, we employ molecular dynamics simulations to investigate the binding dynamics of the PHD finger and bromodomain of BPTF, both in solution and bound to either a histone H3 peptide or a full nucleosome.
View Article and Find Full Text PDFHum Genet
July 2025
Institute of Human Genetics, University Medical Center Göttingen, Heinrich-Düker-Weg 12, 37073, Göttingen, Germany.
FBRSL1-associated syndrome is a rare congenital malformation and intellectual disability syndrome caused by heterozygous truncating variants in Fibrosin-Like 1 (FBRSL1). While FBRSL1 is known to be involved in embryonic development, its precise molecular function remains poorly understood. Therefore, the aim of this study was to elucidate the molecular function of FBRSL1, which is thought to be essential for developmental processes, and to investigate the effect of patient-derived truncating FBRSL1 variants.
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