Intracellular localization of [alpha]-tubulin acetyltransferase ATAT1 in rat ciliated cells

Cilia are microtubule-based hair-like organelles on basal bodies located beneath the cell membrane in various tissues of multicellular animals, and are usually classified into motile cilia and primary cilia. Microtubules are assembled from the heterodimers of [alpha]- and [beta]-tubulin. The lysine residue at position 40 (K40) of [alpha]-tubulin is an important site for acetylation, and this site is acetylated in the cilium. [alpha]-Tubulin N-acetyltransferase 1 (ATAT1) is an acetyltransferase specific to the K40 residue of [alpha]-tubulin; however, its intracellular distribution in mammalian tissues remains unclear. In this study, we analyzed ATAT1 localization in rat trachea, oviduct, kidney, retina, testis and the third ventricle of the brain by immunohistochemical techniques using a specific antibody against ATAT1. ATAT1 was distributed to the motile cilia of multiciliated cells of the trachea, third ventricle of the brain and oviduct, and in the primary cilia of the renal medullary collecting duct. ATAT1 also localized to the primary cilia, inner and outer segments of retinal photoreceptor cells, and at the Golgi apparatus of spermatocytes and spermatids of testis. These results indicated that [alpha]-tubulin acetylation by ATAT1 at distinct subcellular positions may influence the functional regulation of microtubules and cilia in a variety of ciliated cells.