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Literature summary for 2.3.1.108 extracted from

  • Shida, T.; Cueva, J.G.; Xu, Z.; Goodman, M.B.; Nachury, M.V.
    The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation (2010), Proc. Natl. Acad. Sci. USA, 107, 21517-21522.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.108

Protein Variants

Protein Variants Comment Organism
D157N inactive mutant Caenorhabditis elegans

Localization

Localization Comment Organism GeneOntology No. Textmining
microtubule acetylation of alpha-tubulin K40 by alphaTAT1 inside the microtubule lumen Caenorhabditis elegans 5874
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine Caenorhabditis elegans K40 of alpha-tubulin is the sole site of acetylation by alphaTAT1, alphaTAT1 specifically acetylates K40 of alpha-tubulin and prefers microtubules over free tubulin, overview CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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 ?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
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no activity in Potorous tridactylis
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Source Tissue

Source Tissue Comment Organism Textmining
additional information robust alpha-tubulin K40 acetylation in the touch receptor neurons Caenorhabditis elegans
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine K40 of alpha-tubulin is the sole site of acetylation by alphaTAT1, alphaTAT1 specifically acetylates K40 of alpha-tubulin and prefers microtubules over free tubulin, overview Caenorhabditis elegans CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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 ?
acetyl-CoA + [alpha-tubulin]-L-lysine alphaTAT1 acetylates tubulin through its GNAT domain in vitro. K40 of alpha-tubulin is the sole site of acetylation by alphaTAT1. alphaTAT1 displays a greater catalytic efficiency for taxol-stabilized microtubules than for free tubulin Caenorhabditis elegans CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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 ?

Synonyms

Synonyms Comment Organism
alpha-tubulin K40 acetyltransferase
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 Caenorhabditis elegans
alphaTAT1
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 Caenorhabditis elegans
alphaTAT2
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 Caenorhabditis elegans
Mec-17
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 Caenorhabditis elegans

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
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 Caenorhabditis elegans

General Information

General Information Comment Organism
evolution broad phylogenetic distribution of alphaTAT1 Caenorhabditis elegans
malfunction in animals lacking MEC-17, alphaTAT-2, and the sole Caenorhabditis elegans K40 alpha-tubulin MEC-12, touch sensation can be restored by expression of an acetyl-mimic MEC-12 K40Q. Transient overexpression of alphaTAT1 in PtK2 cells is sufficient to acetylate nearly all microtubules, whereas catalytically inactive alphaTAT1 D157N or the HAT Elp3 fail to detectably elevate alpha-tubulin K40 acetylation Caenorhabditis elegans
physiological function alphaTAT1 is the major and possibly the sole alpha-tubulin K40 acetyltransferase in mammals and nematodes, and tubulin acetylation plays a conserved role in several microtubule-based processes. The worm incorporates acetylated alpha-tubulin into their microtubules. alphaTAT1 is required for the acetylation of axonemal microtubules. In Caenorhabditis elegans, microtubule acetylation is most prominent in touch receptor neurons and MEC-17, a homologue of alphaTAT1, and its paralogue alphaTAT-2 are required for alpha-tubulin acetylation and for two distinct types of touch sensation. Worm mechanosensation requires K40 alpha-tubulin acetylation Caenorhabditis elegans