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Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Additionally we are shipping Chromosome 6 Open Reading Frame 134 Antibodies (31) and many more products for this protein.
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Studies indicate that alpha-tubulin (show TUBA4A Proteins) acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6 (show HDAC6 Proteins)).
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 (show LPCAT2 Proteins); 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 (show LPCAT2 Proteins). MEC17 has large, conserved surface patch that is critical for enzymatic activity suggesting extensive interactions with alpha-tubulin (show TUBA4A Proteins).
Mechanistic underpinnings for TAT (show TAT Proteins) activity and its preference for microtubules with slow turnover; cocrystal structures constrain TAT (show TAT Proteins) action to the microtubule lumen with Lys40 engaged in a suboptimal active site; despite the confined location of Lys40, TAT (show TAT Proteins) 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 (show TUBB Proteins) acetylation in vitro and in cells
analysis reveals a basic patch implicated in substrate binding and a conserved glutamine (show GFPT1 Proteins) residue required for catalysis, demonstrating that the family of alpha-tubulin (show TUBA4A Proteins) acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases
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 (show TUBA4A Proteins) is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2 (show SIRT2 Proteins)) and HDAC6 (histone deacetylase 6 (show HDAC6 Proteins)). Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells.
Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus.
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).
hypothetical protein LOC615173
, acetyltransferase mec-17 homolog
, alpha-tubulin N-acetyltransferase
, Novel DUF738 containing protein (2610110G12Rik)
, MEChanosensory abnormality homolog