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DPF2 reads histone lactylation to drive transcription and tumorigenesis [RNA-seq]

ABSTRACT: DPF2 reads histone lactylation to drive transcription and tumorigenesis [RNA-seq]

PROVIDER: PRJNA1109772 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28984813_1.fastq.gz	Fastqsanger.gz
	SRR28984813_2.fastq.gz	Fastqsanger.gz
	SRR28984814_1.fastq.gz	Fastqsanger.gz
	SRR28984814_2.fastq.gz	Fastqsanger.gz

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DPF2 reads histone lactylation to drive transcription and tumorigenesis [CUT&TAG]

Project description:Lysine lactylation (Kla) is a new type of histone mark implicated in the regulation of various functional processes such as transcription. However, how this histone mark acts in cancers remains unexplored due in part to a lack of knowledge about its reader proteins. Here, we observe that cervical cancer (CC) cells undergo metabolic reprogram by which lactate accumulation and thereby boost histone lactylation, particularly H3K14la. Utilizing a multivalent photoaffinity probe in combination with quantitative proteomics approach, we identify DPF2 as a candidate target of H3K14la. Biochemical studies as well as CUT&Tag analysis reveal that DPF2 is capable of binding to H3K14la, and co-localizes with it on promoters of oncogenic genes. Notably, disrupting the association between DPF2 and histone lactylation through structure-guided mutation blunts those cancer-related gene expression along with cell survival. Together, our findings reveal DPF2 as a bona fide H3K14la effector that couples histone lactylation to gene transcription and cell survival, offering insight into how histone Kla engages in transcription and tumorigenesis.

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DPF2 reads histone lactylation to drive transcription and tumorigenesis [RNA-seq]

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