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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 Proteins (7) and many more products for this protein.
Showing 10 out of 33 products:
Cow (Bovine) Polyclonal C6orf134 Primary Antibody for WB - ABIN2775513
Lazrek, Goffard, Schanen, Karquel, Bocket, Lion, Devaux, Hedouin, Gosset, Hober: Detection of hepatitis C virus antibodies and RNA among medicolegal autopsy cases in Northern France. in Diagnostic microbiology and infectious disease 2006
Show all 2 references for 2775513
Cow (Bovine) Polyclonal C6orf134 Primary Antibody for WB - ABIN2775511
Kalebic, Martinez, Perlas, Hublitz, Bilbao-Cortes, Fiedorczuk, Andolfo, Heppenstall: Tubulin acetyltransferase ?TAT1 destabilizes microtubules independently of its acetylation activity. in Molecular and cellular biology 2013
These results suggest that alphaTAT1-mediated Wnt1 (show WNT1 Antibodies) expression via microtubule acetylation is important for colon cancer progression.
Studies indicate that alpha-tubulin (show TUBA4A Antibodies) acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6 (show HDAC6 Antibodies)).
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 Antibodies)) and promote the alpha-tubulin (show TUBA4A Antibodies) 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 Antibodies); 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 Antibodies). MEC17 has large, conserved surface patch that is critical for enzymatic activity suggesting extensive interactions with alpha-tubulin (show TUBA4A Antibodies).
Mechanistic underpinnings for TAT (show TAT Antibodies) activity and its preference for microtubules with slow turnover; cocrystal structures constrain TAT (show TAT Antibodies) action to the microtubule lumen with Lys40 engaged in a suboptimal active site; despite the confined location of Lys40, TAT (show TAT Antibodies) 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 Antibodies) acetylation in vitro and in cells
analysis reveals a basic patch implicated in substrate binding and a conserved glutamine (show GFPT1 Antibodies) residue required for catalysis, demonstrating that the family of alpha-tubulin (show TUBA4A Antibodies) 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 Antibodies) is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2 (show SIRT2 Antibodies)) and HDAC6 (histone deacetylase 6 (show HDAC6 Antibodies)). 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