N-acetyltransferase 9 (NAT9)

N-acetyltransferase 9 (NAT9) is a member of the NAT family that acetylates N-terminal residues of proteins, particularly alpha- and beta-tubulin subunits, thereby contributing to microtubule stability[2][5]. It functions in both an enzyme-dependent and enzyme-independent fashion: its acetylation helps tag proteins for degradation (as in viral host restriction), while its structural interactions regulate stability of microtubules and downstream effects including JNK signaling, apoptosis, and cell survival[1][2][3]. NAT9’s biological roles have been implicated in neurodegenerative disease models, immune response to viral infection, and developmental processes. NAT9 is functionally conserved across species and may represent a novel regulatory node in intracellular signaling and cytoskeletal function[1][2][3][5].

Other names

Alpha/beta-tubulin-N-acetyltransferase 9EBSDKFZP564C103Embryo brain-specific protein (EBSP)hNATLN-acetyltransferase 9 (GCN5-related, putative)

Enzyme inhibition/activation affecting microtubule stability and cell death pathways N-acetylation-mediated protein degradation (e.g., viral glycoprotein GP5 degradation via ubiquitin–proteasome pathway in PRRSV) Downregulation of JNK signaling, reducing cell death