| The alpha-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases. | The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases.
Iuzzolino A, Pellegrini FR, Rotili D, Degrassi F, Trisciuoglio D., Free PMC Article | 05/14/2024 |
| alphaTAT1-induced tubulin acetylation promotes ameloblastoma migration and invasion. | αTAT1-induced tubulin acetylation promotes ameloblastoma migration and invasion.
Yoshimoto S, Morita H, Okamura K, Hiraki A, Hashimoto S., Free PMC Article | 02/19/2022 |
| Microtubule Acetylation Controls MDA-MB-231 Breast Cancer Cell Invasion through the Modulation of Endoplasmic Reticulum Stress. | Microtubule Acetylation Controls MDA-MB-231 Breast Cancer Cell Invasion through the Modulation of Endoplasmic Reticulum Stress.
Ko P, Choi JH, Song S, Keum S, Jeong J, Hwang YE, Kim JW, Rhee S., Free PMC Article | 07/17/2021 |
| The interactions of GCN5L1, RanBP2 and alphaTAT1 function in concert to control alpha-tubulin acetylation and may contribute towards the regulation of cellular lysosome positioning. | GCN5L1 interacts with αTAT1 and RanBP2 to regulate hepatic α-tubulin acetylation and lysosome trafficking.
Wu K, Wang L, Chen Y, Pirooznia M, Singh K, Wälde S, Kehlenbach RH, Scott I, Gucek M, Sack MN., Free PMC Article | 01/11/2020 |
| the actin-MRTF-SRF circuit controls alpha-TAT1 transcription. INF2 regulates the circuit, and hence microtubule acetylation, in cell types where it has a prominent role in actin polymerization. | The actin-MRTF-SRF transcriptional circuit controls tubulin acetylation via α-TAT1 gene expression.
Fernández-Barrera J, Bernabé-Rubio M, Casares-Arias J, Rangel L, Fernández-Martín L, Correas I, Alonso MA., Free PMC Article | 02/23/2019 |
| The specific distributions of ATAT1 through the cell cycle in fibroblasts suggest multiple functions of ATAT1, which could include acetylation of microtubules, RNA transcription activity, severing microtubules, and completion of cytokinesis. | Dynamic localization of α-tubulin acetyltransferase ATAT1 through the cell cycle in human fibroblastic KD cells.
Nekooki-Machida Y, Nakakura T, Nishijima Y, Tanaka H, Arisawa K, Kiuchi Y, Miyashita T, Hagiwara H. | 01/19/2019 |
| these results demonstrate alphaTAT1 enters the lumen of microtubules from open extremities and spreads K40 acetylation marks longitudinally along cellular microtubules; this mode of tip-directed microtubule acetylation may allow for selective acetylation of subsets of microtubules | αTAT1 controls longitudinal spreading of acetylation marks from open microtubules extremities.
Ly N, Elkhatib N, Bresteau E, Piétrement O, Khaled M, Magiera MM, Janke C, Le Cam E, Rutenberg AD, Montagnac G., Free PMC Article | 05/26/2018 |
| Depletion of the tubulin acetyltransferase TAT1 led to a significant increase in the frequency of microtubule breakage. | Microtubules acquire resistance from mechanical breakage through intralumenal acetylation.
Xu Z, Schaedel L, Portran D, Aguilar A, Gaillard J, Marinkovich MP, Théry M, Nachury MV., Free PMC Article | 12/2/2017 |
| cellular quiescence induces Mec17 to couple the production of acetylated microtubules and Myh10, whose accumulation overcomes the inhibitory role of Myh9 and initiates ciliogenesis | A Mec17-Myosin II Effector Axis Coordinates Microtubule Acetylation and Actin Dynamics to Control Primary Cilium Biogenesis.
Rao Y, Hao R, Wang B, Yao TP., Free PMC Article | 10/14/2017 |
| These results suggest that alphaTAT1-mediated Wnt1 expression via microtubule acetylation is important for colon cancer progression. | Genetic disruption of tubulin acetyltransferase, αTAT1, inhibits proliferation and invasion of colon cancer cells through decreases in Wnt1/β-catenin signaling.
Oh S, You E, Ko P, Jeong J, Keum S, Rhee S. | 06/3/2017 |
| Studies indicate that alpha-tubulin acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). | Tubulin acetylation: responsible enzymes, biological functions and human diseases.
Li L, Yang XJ., Free PMC Article | 04/2/2016 |
| Results suggest that lithium chloride (LiCl) treatments activate alpha-tubulin N-acetyltransferase 1 (alphaTAT1) by the inhibition of glycogen synthase kinase 3 beta (GSK-3beta) and promote the alpha-tubulin acetylation, and then elongate the primary cilia. | The elongation of primary cilia via the acetylation of α-tubulin by the treatment with lithium chloride in human fibroblast KD cells.
Nakakura T, Asano-Hoshino A, Suzuki T, Arisawa K, Tanaka H, Sekino Y, Kiuchi Y, Kawai K, Hagiwara H. | 01/16/2016 |
| Data suggest that invariant residues Arg132 and Ser160 in catalytic domain of ATAT1 participate in stable interaction with CoA and acetyl-CoA; ATAT1 with mutation at either residue exhibits much faster intracellular degradation. | Structural basis of cofactor-mediated stabilization and substrate recognition of the α-tubulin acetyltransferase αTAT1.
Yuzawa S, Kamakura S, Hayase J, Sumimoto H. | 05/30/2015 |
| Crystal structure of the catalytic core of human MEC-17 in complex with acetyl-CoA. MEC17 has large, conserved surface patch that is critical for enzymatic activity suggesting extensive interactions with alpha-tubulin. | Structural and functional characterization of the α-tubulin acetyltransferase MEC-17.
Davenport AM, Collins LN, Chiu H, Minor PJ, Sternberg PW, Hoelz A., Free PMC Article | 10/11/2014 |
| Mechanistic underpinnings for TAT activity and its preference for microtubules with slow turnover; cocrystal structures constrain TAT action to the microtubule lumen with Lys40 engaged in a suboptimal active site; despite the confined location of Lys40, TAT efficiently scans the microtubule bidirectionally and acetylates stochastically without preference for ends. | Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase.
Szyk A, Deaconescu AM, Spector J, Goodman B, Valenstein ML, Ziolkowska NE, Kormendi V, Grigorieff N, Roll-Mecak A., Free PMC Article | 08/9/2014 |
| microtubules contacting clathrin-coated pits become acetylated by alphaTAT1; in migrating cells, this mechanism ensures the acetylation of microtubules oriented towards the leading edge, thus promoting directional cell locomotion and chemotaxis | αTAT1 catalyses microtubule acetylation at clathrin-coated pits.
Montagnac G, Meas-Yedid V, Irondelle M, Castro-Castro A, Franco M, Shida T, Nachury MV, Benmerah A, Olivo-Marin JC, Chavrier P., Free PMC Article | 11/30/2013 |
| analysis reveals a basic patch implicated in substrate binding and a conserved glutamine residue required for catalysis, demonstrating that the family of alpha-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases | Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA.
Taschner M, Vetter M, Lorentzen E., Free PMC Article | 02/23/2013 |
| cysteine residues play important catalytic roles through a ternary complex mechanism. alphaTAT1 mutations have analogous effects on tubulin acetylation in vitro and in cells | Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation.
Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R., Free PMC Article | 02/23/2013 |
| Observational study of gene-disease association. (HuGE Navigator) | High-density SNP screening of the major histocompatibility complex in systemic lupus erythematosus demonstrates strong evidence for independent susceptibility regions.
Barcellos LF, May SL, Ramsay PP, Quach HL, Lane JA, Nititham J, Noble JA, Taylor KE, Quach DL, Chung SA, Kelly JA, Moser KL, Behrens TW, Seldin MF, Thomson G, Harley JB, Gaffney PM, Criswell LA., Free PMC Article | 01/20/2010 |