Scholarlink

<p>Enhancer–promoter (E-P) interactions regulate transcription during cell fate determination. However, the regulatory mechanisms underlying E-P interactions have remained elusive. Here we present a chromatin-interaction-based proteomic approach, LoopID, to profile proteins (termed the looposome) at certain E-P anchors. We find that histone demethylase JMJD2, a key looposome component, can regulate E-P interactions and the looposome in a catalytic-independent manner through formation of biomolecular condensates. Furthermore, we introduce a system to engineer E-P interactions by assembling JMJD2 condensates at certain genomic loci, enabling construction of cell-type-specific E-P interactions to promote cellular reprogramming into pluripotent or two-cell-like cells. Our findings reveal a noncanonical function of a histone demethylase in regulation of chromatin organization and provide a strategy to regulate cell fate transitions through E-P interactions.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

JMJD2 regulates enhancer–promoter interactions via biomolecular condensate formation

  • 期刊论文

  • 发表日期：

    2025年12月16日

查看全文
  • Shaoshuai Jiang,
  • Xinyi Liu,
  • Zhuheng Zhang,
  • Mingzhu Yang,
  • Xing Zhu,
  • Lin Ma,
  • Longying Zhao,
  • Xiaoru Ling,
  • Ziqiang Zhou,
  • Ziqiang Wu,
  • Jiale Qu,
  • Haochen Li,
  • Jiawei Liang,
  • Zhiheng Deng,
  • Qi Tian,
  • Xiaona Huang,
  • Xianglin Huang,
  • Jin Tan,
  • Jun Sun,
  • Jia Wang,
  • Diana Guallar,
  • Partha Pratim Das,
  • Luca Pinello,
  • Liang Wang,
  • Hongfu Wu,
  • Dong-feng Huang,
  • Jichang Wang,
  • Hancheng Lin,
  • Jin Bai,
  • Lili Fan,
  • Wei Chi,
  • Xue Xiao,
  • Junjun Ding

摘要

Enhancer–promoter (E-P) interactions regulate transcription during cell fate determination. However, the regulatory mechanisms underlying E-P interactions have remained elusive. Here we present a chromatin-interaction-based proteomic approach, LoopID, to profile proteins (termed the looposome) at certain E-P anchors. We find that histone demethylase JMJD2, a key looposome component, can regulate E-P interactions and the looposome in a catalytic-independent manner through formation of biomolecular condensates. Furthermore, we introduce a system to engineer E-P interactions by assembling JMJD2 condensates at certain genomic loci, enabling construction of cell-type-specific E-P interactions to promote cellular reprogramming into pluripotent or two-cell-like cells. Our findings reveal a noncanonical function of a histone demethylase in regulation of chromatin organization and provide a strategy to regulate cell fate transitions through E-P interactions.