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Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Zusätzlich bieten wir Ihnen Chromosome 6 Open Reading Frame 134 Antikörper (37) und viele weitere Produktgruppen zu diesem Protein an.
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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.
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
Depletion of the tubulin acetyltransferase TAT1 led to a significant increase in the frequency of microtubule breakage.
cellular quiescence induces Mec17 to couple the production of acetylated microtubules and Myh10, whose accumulation overcomes the inhibitory role of Myh9 and initiates ciliogenesis
These results suggest that alphaTAT1-mediated Wnt1 expression via microtubule acetylation is important for colon cancer progression.
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).
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.
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.
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.
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.
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
cysteine residues play important catalytic roles through a ternary complex mechanism. alphaTAT1 mutations have analogous effects on tubulin acetylation in vitro and in cells
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
Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus.
TAK1 directly interacts with and phosphorylates alphaTAT1 at Ser237 to critically enhance its catalytic activity.
Atat1 knockdown resulted in a significant increase in the expression of ACTH-producing genes and decreased the dexamethasone-induced nuclear translocation of glucocorticoid receptor accompanied with a reduction in alpha-tubulin acetylation.
Here the authors demonstrate that mice lacking the alpha-tubulin acetyltransferase Atat1 in sensory neurons display profound deficits in their ability to detect mechanical stimuli.
alphaTAT1 has a conserved function as the major alpha-tubulin acetyltransferase in ciliated organisms and has an important role in regulating subcellular specialization of subsets of microtubules.
Data indicate that alpha-tubulin acetyltransferase 1 Atat1 is not required for survival and development but may regulate more advanced functions.
Acetylation of alpha-tubulin is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2) and HDAC6 (histone deacetylase 6). Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells.
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development (By similarity).
acetyltransferase mec-17 homolog
, alpha-tubulin N-acetyltransferase
, MEChanosensory abnormality homolog
, Novel DUF738 containing protein (2610110G12Rik)
, alpha-tubulin N-acetyltransferase 1