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Nuclear PD-L1 compartmentalization suppresses tumorigenesis and overcomes immunocheckpoint therapy resistance in mice via histone macroH2A1.
J Clin Invest
November 2024
Department of Otolaryngology Head and Neck Surgery, Xiangya Hospital, Central South University, Changsha, China.
Canonically PD-L1 functions as the inhibitory immune checkpoint on cell surface. Recent studies have observed PD-L1 expression in the nucleus of cancer cells. But the biological function of nuclear PD-L1 (nPD-L1) in tumor growth and antitumor immunity is unclear.
View Article and Find Full Text PDFIdentification of a novel DNA oxidative damage repair pathway, requiring the ubiquitination of the histone variant macroH2A1.1.
BMC Biol
September 2024
Département de Génomique Fonctionnelle Et Cancer, Institut de Génétique Et Biologie Moléculaire Et Cellulaire (IGBMC), Université de Strasbourg/CNRS/INSERM, Equipe Labellisée La Ligue Nationale Contre Le Cancer, 67404, Illkirch Cedex, France.
Background: The histone variant macroH2A (mH2A), the most deviant variant, is about threefold larger than the conventional histone H2A and consists of a histone H2A-like domain fused to a large Non-Histone Region responsible for recruiting PARP-1 to chromatin. The available data suggest that the histone variant mH2A participates in the regulation of transcription, maintenance of heterochromatin, NAD metabolism, and double-strand DNA repair.
Results: Here, we describe a novel function of mH2A, namely its implication in DNA oxidative damage repair through PARP-1.
Histone variant macroH2A1 regulates synchronous firing of replication origins in the inactive X chromosome.
Nucleic Acids Res
October 2024
Cell Biology and Epigenetics, Department of Biology, Technical University of Darmstadt, 64287 Darmstadt, Germany.
MacroH2A has been linked to transcriptional silencing, cell identity, and is a hallmark of the inactive X chromosome (Xi). However, it remains unclear whether macroH2A plays a role in DNA replication. Using knockdown/knockout cells for each macroH2A isoform, we show that macroH2A-containing nucleosomes slow down replication progression rate in the Xi reflecting the higher nucleosome stability.
View Article and Find Full Text PDFA FACT about macroH2A removal in immune gene activation.
Mol Cell
August 2024
Program of Applied Epigenetics, Program of Myeloid Neoplasms, Josep Carreras Leukaemia Research Institute (IJC), Campus Can Ruti, Badalona, Spain; Germans Trias i Pujol Research Institute (IGTP), Badalona, Spain. Electronic address:
Histone variants contribute to epigenetic regulation in development and disease but require the chaperone machinery for correct deposition. In this issue of Molecular Cell, Ji et al. explain how the chaperone complex FACT removes the histone variant macroH2A1.
View Article and Find Full Text PDFFACT mediates the depletion of macroH2A1.2 to expedite gene transcription.
Mol Cell
August 2024
Department of Immunology, School of Basic Medical Sciences, Beijing Key Laboratory for Tumor Invasion and Metastasis, Capital Medical University, Beijing 100069, China; Beijing Institute of Hepatology, Beijing Youan Hospital, Capital Medical University, Beijing 100069, China. Electronic address:
The histone variant macroH2A is generally linked to transcriptionally inactive chromatin, but how macroH2A regulates chromatin structure and functions in the transcriptional process remains elusive. This study reveals that while the integration of human macroH2A1.2 into nucleosomes does not affect their stability or folding dynamics, it notably hinders the maintenance of facilitates chromatin transcription's (FACT's) function.
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