MEC-17 is an α-tubulin acetyltransferase

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Structural and functional characterization of the α-tubulin acetyltransferase MEC-17.

Tubulin protomers undergo an extensive array of post-translational modifications to tailor microtubules to specific tasks. One such modification, the acetylation of lysine 40 of α-tubulin, located in the lumen of microtubules, is associated with stable, long-living microtubule structures. MEC-17 was recently identified as the acetyltransferase that mediates this event. We have determined the cr...

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Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin.

Cytoskeleton remodelling is a prerequisite step for the morphological transition from preadipocytes to mature adipocytes. Although microtubules play a pivotal role in organizing cellular structure, regulation of microtubule dynamics during adipogenesis remains unclear. In the present paper we show that acetylation of α-tubulin is up-regulated during adipogenesis, and adipocyte development is de...

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Genetically Separable Functions of the MEC-17 Tubulin Acetyltransferase Affect Microtubule Organization

BACKGROUND Microtubules (MTs) are formed from the lateral association of 11-16 protofilament chains of tubulin dimers, with most cells containing 13-protofilament (13-p) MTs. How these different MTs are formed is unknown, although the number of protofilaments may depend on the nature of the α- and β-tubulins. RESULTS Here we show that the enzymatic activity of the Caenorhabiditis elegans α-tu...

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MEC-17 deficiency leads to reduced α-tubulin acetylation and impaired migration of cortical neurons.

Neuronal migration is a fundamental process during the development of the cerebral cortex and is regulated by cytoskeletal components. Microtubule dynamics can be modulated by posttranslational modifications to tubulin subunits. Acetylation of α-tubulin at lysine 40 is important in regulating microtubule properties, and this process is controlled by acetyltransferase and deacetylase. MEC-17 is ...

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Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation.

Protein acetylation is an important posttranslational modification with the recent identification of new substrates and enzymes, new links to disease, and modulators of protein acetylation for therapy. α-Tubulin acetyltransferase (αTAT1) is the major α-tubulin lysine-40 (K40) acetyltransferase in mammals, nematodes, and protozoa, and its activity plays a conserved role in several microtubule-ba...

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ژورنال

عنوان ژورنال: Nature

سال: 2010

ISSN: 0028-0836,1476-4687

DOI: 10.1038/nature09324