Core Viewpoint - The research published in Nature Genetics reveals the role of JMJD2 in regulating enhancer-promoter interactions through biomolecular condensate formation, providing new insights into gene transcription regulation and cellular fate determination [2][5]. Group 1: Research Findings - The study introduces a novel proteomics method called LoopID, which identifies specific chromatin interaction components (looposome) and is the only chromatin structure-based proteomics approach available [2][5]. - JMJD2, a histone demethylase, is identified as a key component of the looposome, regulating enhancer-promoter interactions and looposome function in a non-catalytic manner through biomolecular condensate formation [5]. - The research team developed a system to engineer enhancer-promoter interactions by assembling JMJD2 condensates at specific genomic loci, facilitating cell type-specific enhancer-promoter interactions to promote reprogramming into pluripotent or intermediate cell states [5]. Group 2: Implications - The findings highlight a non-classical function of histone demethylases in chromatin organization regulation, offering new strategies for manipulating cellular fate transitions via enhancer-promoter interactions [5].