MEC-17 is an α-tubulin acetyltransferase

Jyothi S. Akella, Dorota Wloga, Jihyun Kim, Natalia G. Starostina, Sally Lyons-Abbott, Naomi S. Morrissette, Scott T. Dougan, Edward T. Kipreos and Jacek Gaertig ()
Additional contact information
Jyothi S. Akella: University of Georgia
Dorota Wloga: University of Georgia
Jihyun Kim: University of Georgia
Natalia G. Starostina: University of Georgia
Sally Lyons-Abbott: University of California
Naomi S. Morrissette: University of California
Scott T. Dougan: University of Georgia
Edward T. Kipreos: University of Georgia
Jacek Gaertig: University of Georgia

Nature, 2010, vol. 467, issue 7312, 218-222

Abstract: MEC1-7 is long-sought α-tubulin acetyltransferase It has long been known that in a subset of microtubules, α-tubulin is modified post-translationally by acetylation of lysine-40. There is growing evidence that this highly conserved microtubule modification is a key event during cell polarization, especially in the nervous system. The enzyme responsible for this reaction has now been identified as MEC-17, a protein related to the Gcn5 histone receptor acetyltransferase and required for the function of touch receptor neurons in Caenorhabditis elegans.

Date: 2010
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DOI: 10.1038/nature09324

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