ArticleMedical molecular morphology2016
Intracellular localization of α-tubulin acetyltransferase ATAT1 in rat ciliated cells.
Article in Medical molecular morphology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- TGFβ signaling regulates Col15a1 expression in fenestrated endothelial cells of the rat pituitary.Cell and tissue research · 2026Article
- Regulation of Aqp1 expression by osmotic balance in fenestrated endothelial cells of the posterior lobe of the pituitary.Cell and tissue research · 2025Article
- Review
- Expression and localization of alpha-tubulin N-acetyltransferase 1 in the reproductive system of male mice.The Journal of reproduction and development · 2021Article
- Fibronectin is essential for formation of fenestrae in endothelial cells of the fenestrated capillary.Cell and tissue research · 2021Article
- Loss of Deacetylation Enzymes Hdac6 and Sirt2 Promotes Acetylation of Cytoplasmic Tubulin, but Suppresses Axonemal Acetylation in Zebrafish Cilia.Frontiers in cell and developmental biology · 2021Article
- Role of tubulin acetylation in cellular functions and diseases.Medical molecular morphology · 2020Review
- Article
- Localization of Mucin 1 in endometrial luminal epithelium and its expression in women with reproductive failure during implantation window.Journal of molecular histology · 2019Article
- Dynamic localization of α-tubulin acetyltransferase ATAT1 through the cell cycle in human fibroblastic KD cells.Medical molecular morphology · 2018Article
- Expression and localization of forkhead box protein FOXJ1 in S100β-positive multiciliated cells of the rat pituitary.Medical molecular morphology · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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