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Histone Variants at the Centromere02:30

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The Histone Modifier KANSL2 Is an Actionable Biomarker in Multiple Myeloma.

Kaiting Jiang1, Marieluise Kirchner2, Frederik Herzberg1

  • 1Department of Hematology, Oncology and Cancer Immunology, Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin Berlin, Germany.

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|November 26, 2025
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Multiple myeloma (MM) cells rely on KANSL2 for survival against stress. Targeting KANSL2 with specific epigenetic drugs shows promise for overcoming chemotherapy resistance in MM patients.

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Area of Science:

  • Oncology
  • Epigenetics
  • Molecular Biology

Background:

  • Epigenetic alterations are crucial in multiple myeloma (MM) pathogenesis.
  • Targeted therapies for MM based on epigenetic modifications are lacking.
  • Identifying novel oncogenes and therapeutic targets in MM is essential.

Purpose of the Study:

  • To identify novel epigenetic targets in multiple myeloma.
  • To investigate the role of KAT8 regulatory NSL complex subunit 2 (KANSL2) in MM.
  • To evaluate KANSL2 as a potential therapeutic biomarker for MM.

Main Methods:

  • Integration of clinical and molecular MM patient data.
  • Unbiased genetic in vivo screening.
  • Genetic gain and loss of function models.
  • Transcriptomics, proteomics, and quantitative acetylome profiling.
  • Ex vivo drug response profiling in patient samples.

Main Results:

  • KANSL2 identified as a candidate oncogene associated with adverse MM prognosis.
  • KANSL2 confers protection against genotoxic stress.
  • A KANSL2-dependent molecular program was identified, targetable by acetylation modifiers.
  • High KANSL2 expression correlated with increased sensitivity to HDAC and BET inhibitors.
  • KANSL2 expression predicted selective MM cell killing by these inhibitors in patient samples.

Conclusions:

  • KANSL2 is a mediator of chemotherapy resistance in multiple myeloma.
  • KANSL2 serves as an actionable biomarker for response to epigenetic therapies.
  • Targeting the KANSL2-dependent epigenetic program offers a novel therapeutic strategy for MM.