title: Intracellular localization of α-tubulin acetyltransferase ATAT1 in rat ciliated cells.
abstract: 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 α- and β-tubulin. The lysine residue at position 40 (K40) of α-tubulin is an important site for acetylation, and this site is acetylated in the cilium. α-Tubulin N-acetyltransferase 1 (ATAT1) is an acetyltransferase specific to the K40 residue of α-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 α-tubulin acetylation by ATAT1 at distinct subcellular positions may influence the functional regulation of microtubules and cilia in a variety of ciliated cells.
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan. nakakura@med.teikyo-u.ac.jp.
authors.forename: Takashi
authors.initials: T
authors.lastname: Nakakura
authors.affiliation: Department of Biology, Sapporo Medical University, Sapporo, Japan.
authors.forename: Takeshi
authors.initials: T
authors.lastname: Suzuki
authors.affiliation: Department of Physiology, Nippon Medical School, Tokyo, Japan.
authors.forename: Takahiro
authors.initials: T
authors.lastname: Nemoto
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan.
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Tanaka
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan.
authors.forename: Anshin
authors.initials: A
authors.lastname: Asano-Hoshino
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan.
authors.forename: Kenjiro
authors.initials: K
authors.lastname: Arisawa
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan.
authors.forename: Yoshimi
authors.initials: Y
authors.lastname: Nishijima
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan.
authors.forename: Yoshiko
authors.initials: Y
authors.lastname: Kiuchi
authors.affiliation: Department of Anatomy, Graduate School of Medicine, Teikyo University, 2-11-1 Kaga Itabashi-Ku, Tokyo, 173-8605, Japan.
authors.forename: Haruo
authors.initials: H
authors.lastname: Hagiwara
mesh_terms: D000123:Acetyltransferases / Q000378:metabolism*; D000818:Animals; D000918:Antibody Specificity / Q000276:immunology; D015153:Blotting, Western; D002923:Cilia / Q000201:enzymology* / Q000648:ultrastructure; D005260:Female; D006801:Humans; D042541:Intracellular Space / Q000378:metabolism*; D008297:Male; D009928:Organ Specificity; D017208:Rats, Wistar
chemical_list: D000123:Acetyltransferases; C049182:alpha-tubulin acetylase
keywords: ATAT1; Acetylation; Cilia; Microtubule; α-Tubulin