N-alpha-acetyltransferase 80 (NAA80)

N-alpha-acetyltransferase 80 (NAA80) is a cytoplasmic enzyme that specifically catalyzes the posttranslational N-terminal acetylation of mature actin, a modification essential for normal actin filament dynamics and cell morphology[2][1][3][4]. Unlike other N-acetyltransferases, NAA80 acts after initial processing by NatB and removal of initiator methionine, transferring an acetyl group to actin’s N-terminus enriched in acidic residues[1][2]. Its unique substrate specificity is conferred by an open substrate binding region that accommodates actin’s N-terminus[1][3]. NAA80’s activity is regulated by the actin chaperone profilin, which enhances NAA80’s catalytic efficiency toward monomeric actin and aligns the actin N-terminus within the enzyme’s groove[4]. Genetic localization places the NAA80 gene within a tumor suppressor region, and although its direct links to disease are under investigation, altered NAA80 function may contribute to abnormalities in cell migration relevant to cancer metastasis[2]. Experimental inhibitors have been developed to target NAA80 for research into cytoskeletal regulation, but there are currently no approved therapeutic drugs targeting the enzyme[1].

Other names

N-acetyltransferase 80NatH catalytic subunitNAT6FUS2HsNAAA80Protein fus-2N-acetyltransferase 6Protein fusion-2ANDSFUS-2

Catalytic transfer of an acetyl group from acetyl-CoA to the N-terminus of actin after initial methionine removal Inhibition of NAA80 produces hypomodified actin with consequences to filament dynamics[1]