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Immunoprecipitation and mass spectrometry (IP-MS) on KAT6A chimeras

ABSTRACT: Despite KAT6A chimeras potent oncogenic activity, the mechanisms by which KAT6A fusion proteins achieve genomic specificity and drive leukemogenesis remain poorly understood. Previous studies suggest that the leukemogenic potential of KAT6A-TIF2 depends on its chromatin-binding ability rather than its histone acetyltransferase (HAT) activity, with oncogenicity further amplified by CBP recruitment through its fusion partners. The winged helix domain (WH1) of KAT6A can bind unmethylated CpG islands and interact with P300/CBP via the TAZ2 domain. However, the widespread presence of unmethylated CpG islands across the genome does not fully explain the genomic specificity of KAT6A-CBP (K/C) and KAT6A-P300 (K/P) fusions, leaving key mechanistic gaps unexplored. To uncover protein interactions underlying these genomic associations, we performed immunoprecipitation and mass spectrometry (IP-MS) on KAT6A N-terminus and chimeras. Mass spectrometry analysis was performed to identify the core components of the KAT6A complex and the interacting proteins of KAT6A.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hek-293t Cell

SUBMITTER: Junhui Lv

LAB HEAD: Kaiwei Liang

PROVIDER: PXD061491 | Pride | 2025-08-08

REPOSITORIES: Pride

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			Action	DRS
	KAT6A_CBP.msf	Msf
	KAT6A_CBP_1.raw	Raw
	KAT6A_CBP_2.raw	Raw
	KAT6A_CBP_3.raw	Raw
	KAT6A_NCOA3.msf	Msf

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