m6A modulates neuronal functions and sex determination in Drosophila

Tina Lence, Junaid Akhtar, Marc Bayer, Katharina Schmid, Laura Spindler, Cheuk Hei Ho, Nastasja Kreim, Miguel A. Andrade-Navarro, Burkhard Poeck, Mark Helm and Jean-Yves Roignant ()
Additional contact information
Tina Lence: Institute of Molecular Biology (IMB)
Junaid Akhtar: Institute of Molecular Biology (IMB)
Marc Bayer: Institute of Molecular Biology (IMB)
Katharina Schmid: Institute of Pharmacy and Biochemistry, Johannes Gutenberg University of Mainz
Laura Spindler: Institute of Zoology III (Neurobiology), Johannes Gutenberg University of Mainz
Cheuk Hei Ho: Kimmel Center for Biology and Medicine of the Skirball Institute, NYU School of Medicine
Nastasja Kreim: Institute of Molecular Biology (IMB)
Miguel A. Andrade-Navarro: Institute of Molecular Biology (IMB)
Burkhard Poeck: Institute of Zoology III (Neurobiology), Johannes Gutenberg University of Mainz
Mark Helm: Institute of Pharmacy and Biochemistry, Johannes Gutenberg University of Mainz
Jean-Yves Roignant: Institute of Molecular Biology (IMB)

Nature, 2016, vol. 540, issue 7632, 242-247

Abstract: Abstract N6-methyladenosine RNA (m6A) is a prevalent messenger RNA modification in vertebrates. Although its functions in the regulation of post-transcriptional gene expression are beginning to be unveiled, the precise roles of m6A during development of complex organisms remain unclear. Here we carry out a comprehensive molecular and physiological characterization of the individual components of the methyltransferase complex, as well as of the YTH domain-containing nuclear reader protein in Drosophila melanogaster. We identify the member of the split ends protein family, Spenito, as a novel bona fide subunit of the methyltransferase complex. We further demonstrate important roles of this complex in neuronal functions and sex determination, and implicate the nuclear YT521-B protein as a main m6A effector in these processes. Altogether, our work substantially extends our knowledge of m6A biology, demonstrating the crucial functions of this modification in fundamental processes within the context of the whole animal.

Date: 2016
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DOI: 10.1038/nature20568

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