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Interaction proteins with KAT6A

ABSTRACT: Lysine acetyltransferases (KATs) catalyze the transfer of acetyl groups from acetyl-CoA to lysine residues. Our proteomic analysis revealed that KAT6A is acetylated at lysine 815 (K815), corresponding to mouse K816, in the hearts of mice fed a ketogenic diet under high blood pressure. To identify changes in KAT6A interaction partners by K815 acetylation in cardiomyocytes, we performed LC-MS/MS proteomics. We transfected adenovirus-carrying FLAG-KAT6A-wild type (WT, Control (Ctrl)), -K815R (an acetylation resistant mutant, KR), and -K815Q (an acetylation mimetic mutant, KQ) into cardiomyocytes for 2 days. Adenovirus-carrying FLAG was used as a control. KAT6A was immunoprecipitated with anti-FLAG affinity beads, followed by washing, competitive elution with 3x FLAG peptides, and separation by SDS-PAGE.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Heart, Primary Cell, Cardiac Muscle Cell

SUBMITTER: Michinari Nakamura

LAB HEAD: Michinari Nakamura

PROVIDER: PXD059838 | Pride | 2025-11-03

REPOSITORIES: Pride

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			Action	DRS
	Comparison_Spectra_count.mzML	Mzml
	Comparison_Spectra_count.mzid.gz	Mzid
	Michi_Ctrl_040119.raw	Raw
	Michi_Q_040119.raw	Raw
	Michi_R_040119.raw	Raw

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Publications

KAT6A acetylation regulates AMPK function and hypertrophic remodeling in the heart.

Keller Mariko Aoyagi MA Ivessa Andreas A Liu Tong T Li Hong H Romanienko Peter J PJ Nakamura Michinari M

Molecular metabolism 20250825

Diets influence metabolism and disease susceptibility, with lysine acetyltransferases (KATs) serving as key regulators through acetyl-CoA. We have previously demonstrated that a ketogenic diet alleviates cardiac pathology, though the underlying mechanisms remain largely unknown. Here we show that KAT6A acetylation is crucial for mitochondrial function and cell growth. Proteomic analysis revealed that KAT6A is acetylated at lysine (K)816 in the hearts of mice fed a ketogenic diet under hypertensi ...[more]

PMID: 40865637

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