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MEC-17 is an α-tubulin acetyltransferase

Author

Listed:
  • 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)

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.

Suggested Citation

  • Jyothi S. Akella & Dorota Wloga & Jihyun Kim & Natalia G. Starostina & Sally Lyons-Abbott & Naomi S. Morrissette & Scott T. Dougan & Edward T. Kipreos & Jacek Gaertig, 2010. "MEC-17 is an α-tubulin acetyltransferase," Nature, Nature, vol. 467(7312), pages 218-222, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7312:d:10.1038_nature09324
    DOI: 10.1038/nature09324
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