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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 (33) and Chromosome 6 Open Reading Frame 134 Proteins (7) and many more products for this protein.
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 (show MYH10 ELISA Kits), whose accumulation overcomes the inhibitory role of Myh9 (show MYH9 ELISA Kits) and initiates ciliogenesis
These results suggest that alphaTAT1-mediated Wnt1 (show WNT1 ELISA Kits) expression via microtubule acetylation is important for colon cancer progression.
Studies indicate that alpha-tubulin (show TUBA4A ELISA Kits) acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6 (show HDAC6 ELISA Kits)).
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 (show GSK3b ELISA Kits)) and promote the alpha-tubulin (show TUBA4A ELISA Kits) 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 ELISA Kits); 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 ELISA Kits). MEC17 has large, conserved surface patch that is critical for enzymatic activity suggesting extensive interactions with alpha-tubulin (show TUBA4A ELISA Kits).
Mechanistic underpinnings for TAT (show TAT ELISA Kits) activity and its preference for microtubules with slow turnover; cocrystal structures constrain TAT (show TAT ELISA Kits) action to the microtubule lumen with Lys40 engaged in a suboptimal active site; despite the confined location of Lys40, TAT (show TAT ELISA Kits) 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 ELISA Kits) acetylation in vitro and in cells
Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus.
Here the authors demonstrate that mice lacking the alpha-tubulin (show TUBA4A ELISA Kits) 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 (show TUBA4A ELISA Kits) is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2 (show SIRT2 ELISA Kits)) and HDAC6 (histone deacetylase 6 (show HDAC6 ELISA Kits)). 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