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DPF2 reads histone lactylation to drive transcription and tumorigenesis

ABSTRACT: Identification of hPTM binder through the chemoproteomic approach

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Feng Zhai

LAB HEAD: Guijin Zhai

PROVIDER: PXD051995 | Pride | 2024-12-23

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	H3K14-1.raw	Raw
	H3K14-2.raw	Raw
	H3K14-3.raw	Raw
	H3K14la-1.raw	Raw
	H3K14la-2.raw	Raw

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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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The raw data of competitive chemoproteomic experiments for validating the effectiveness of iTarget.

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