ATAT1 Antibody

1. 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 PMID: 27752143
2. Depletion of the tubulin acetyltransferase TAT1 led to a significant increase in the frequency of microtubule breakage. PMID: 28428427
3. cellular quiescence induces Mec17 to couple the production of acetylated microtubules and Myh10, whose accumulation overcomes the inhibitory role of Myh9 and initiates ciliogenesis PMID: 25494100
4. These results suggest that alphaTAT1-mediated Wnt1 expression via microtubule acetylation is important for colon cancer progression. PMID: 27836544
5. 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). PMID: 26227334
6. 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. PMID: 24760594
7. 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. PMID: 25602620
8. 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. PMID: 24846647
9. 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. PMID: 24906155
10. 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 PMID: 24097348
11. cysteine residues play important catalytic roles through a ternary complex mechanism. alphaTAT1 mutations have analogous effects on tubulin acetylation in vitro and in cells PMID: 23071314
12. 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 PMID: 23071318

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HGNC: 21186

OMIM: 615556

KEGG: hsa:79969

STRING: 9606.ENSP00000327832

UniGene: Hs.654798